White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065435   1 PRTMTQKQKMQRVDqviqDLSLGKCQNTIIGVPgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQV 80
Cdd:cd03234   111 PRKSSDAIRKKRVE----DVLLRDLALTRIGGN-LVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVST 185

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1151065435  81 LKKLSQRGKTVILTIHQPSSELFELFDKILLM 112
Cdd:cd03234   186 LSQLARRNRIVILTIHQPRSDLFRLFDRILLL 217

ABC-type multidrug transport system, ATPase component [Defense mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065435   4 MTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKK 83
Cdd:COG1131   103 LPRKEARERIDELLELFGLTDAADR------KVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRE 176

                          90       100
                  ....*....|....*....|....*....
gi 1151065435  84 LSQRGKTVILTIHQPsSELFELFDKILLM 112
Cdd:COG1131   177 LAAEGKTVLLSTHYL-EEAERLCDRVAII 204

zinc ABC transporter ATP-binding protein AztA;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065435  35 RVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQP 98
Cdd:NF040873  116 QLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDL 179

ribosome-associated ATPase/putative transporter RbbA;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065435  11 QRVDQVIQDLSLGKCQNTiigVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 70
Cdd:NF033858  376 ARVAEMLERFDLADVADA---LPDS---LPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065435   26 QNTIIGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQ------VLKKLSQRGKTVILTIHQP- 98
Cdd:smart00382  48 QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLLLLKSEKNLTVILTTNDEk 127

                           90
                   ....*....|....*..
gi 1151065435   99 ---SSELFELFDKILLM 112
Cdd:smart00382 128 dlgPALLRRRFDRRIVL 144

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065435   1 PRTMTQKQKMQRVDqviqDLSLGKCQNTIIGVPgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQV 80
Cdd:cd03234   111 PRKSSDAIRKKRVE----DVLLRDLALTRIGGN-LVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVST 185

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1151065435  81 LKKLSQRGKTVILTIHQPSSELFELFDKILLM 112
Cdd:cd03234   186 LSQLARRNRIVILTIHQPRSDLFRLFDRILLL 217

ABC transporter G-25; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065435   1 PRTMTQKQKMQRVDQVIQDLSLGKCQNTIIGvPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQV 80
Cdd:PLN03211  170 PKSLTKQEKILVAESVISELGLTKCENTIIG-NSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLT 248

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1151065435  81 LKKLSQRGKTVILTIHQPSSELFELFDKILLM 112
Cdd:PLN03211  249 LGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVL 280

ABC transporter G family member; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065435    1 PRTMTQKQKMQRVDQVIQDLSLGKCQNTIIGVPGrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQV 80
Cdd:PLN03140   983 PKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPG-VTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRT 1061

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1151065435   81 LKKLSQRGKTVILTIHQPSSELFELFDKILLM 112
Cdd:PLN03140  1062 VRNTVDTGRTVVCTIHQPSIDIFEAFDELLLM 1093

ABC-type multidrug transport system, ATPase component [Defense mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065435   4 MTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKK 83
Cdd:COG1131   103 LPRKEARERIDELLELFGLTDAADR------KVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRE 176

                          90       100
                  ....*....|....*....|....*....
gi 1151065435  84 LSQRGKTVILTIHQPsSELFELFDKILLM 112
Cdd:COG1131   177 LAAEGKTVLLSTHYL-EEAERLCDRVAII 204

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065435  11 QRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKT 90
Cdd:cd03225   113 ERVEEALELVGLEGLRDR------SPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKT 186

                          90       100
                  ....*....|....*....|..
gi 1151065435  91 VILTIHQPsSELFELFDKILLM 112
Cdd:cd03225   187 IIIVTHDL-DLLLELADRVIVL 207

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065435  39 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQPsSELFELFDKILLM 112
Cdd:cd03230    96 LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHIL-EEAERLCDRVAIL 168

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065435  36 VKGLSGGERKRLAFAsEALTDPPLLIC-DEPTSGLDSFMAASVVQVLKKLSQR-GKTVILTIHQPSSELFELFDKILLM 112
Cdd:cd03233   116 VRGISGGERKRVSIA-EALVSRASVLCwDNSTRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVL 193

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065435  38 GLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQR-GKTVILTIHQPsSELFELFDKILLM 112
Cdd:cd03229   100 GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDL-DEAARLADRVVVL 174

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065435  39 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQPSSeLFELFDKILLM 112
Cdd:cd03235   133 LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLL 205

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065435  13 VDQVIQDLSLGkcQNTIIGVPGRvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQrGKTVI 92
Cdd:TIGR02857 437 LDEFVAALPQG--LDTPIGEGGA--GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVL 511

                          90       100
                  ....*....|....*....|
gi 1151065435  93 LTIHQPssELFELFDKILLM 112
Cdd:TIGR02857 512 LVTHRL--ALAALADRIVVL 529

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065435  11 QRVDQVIQDLSLGKCQNTIIGvpgrvkGLSGGERKRLAFAsEAL-TDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGK 89
Cdd:COG1121   118 EAVDEALERVGLEDLADRPIG------ELSGGQQQRVLLA-RALaQDPDLLLLDEPFAGVDAATEEALYELLRELRREGK 190

                          90       100
                  ....*....|....*....|...
gi 1151065435  90 TVILTIHQPsSELFELFDKILLM 112
Cdd:COG1121   191 TILVVTHDL-GAVREYFDRVLLL 212

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065435   12 RVDQVIQDLSLGKCQNTIIGvPGRVKGLSGGERKRLAFAsEALTDPPLLIC-DEPTSGLDSFMAASVVQVLKKLSQRGK- 89
Cdd:TIGR00956  184 IADVYMATYGLSHTRNTKVG-NDFVRGVSGGERKRVSIA-EASLGGAKIQCwDNATRGLDSATALEFIRALKTSANILDt 261

                           90       100
                   ....*....|....*....|...
gi 1151065435   90 TVILTIHQPSSELFELFDKILLM 112
Cdd:TIGR00956  262 TPLVAIYQCSQDAYELFDKVIVL 284

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065435  12 RVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTV 91
Cdd:COG4133   111 AIDEALEAVGLAGLADL------PVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAV 184

                  ....*..
gi 1151065435  92 ILTIHQP 98
Cdd:COG4133   185 LLTTHQP 191

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065435   9 KMQRVDQVIQDLSLGkcQNTIIGVPGRvkGLSGGERKRLAFAsEAL-TDPPLLICDEPTSGLDSFMAASVVQVLKKLSQR 87
Cdd:COG4618   442 KLAGVHEMILRLPDG--YDTRIGEGGA--RLSGGQRQRIGLA-RALyGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR 516

                          90       100
                  ....*....|....*....|....*
gi 1151065435  88 GKTVILTIHQPSseLFELFDKILLM 112
Cdd:COG4618   517 GATVVVITHRPS--LLAAVDKLLVL 539

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065435  39 LSGGERKRLAFASeALT-DPPLLICDEPTSGLDSFMAASVVQVLKKLS-QRGKTVILTIHQPSSELfELFDKILLM 112
Cdd:cd03214    98 LSGGERQRVLLAR-ALAqEPPILLLDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAA-RYADRVILL 171

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151065435  38 GLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHqpSSELFE 104
Cdd:cd03292   136 ELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH--AKELVD 200

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065435  12 RVDQVIQDLSLGkcQNTIIGVPGRvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSqRGKTV 91
Cdd:COG1132   454 QAHEFIEALPDG--YDTVVGERGV--NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTT 528

                          90       100
                  ....*....|....*....|.
gi 1151065435  92 ILTIHQPSSelFELFDKILLM 112
Cdd:COG1132   529 IVIAHRLST--IRNADRILVL 547

ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1151065435  39 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQR-GKTVILTIHQpSSELFELFDKILLM 112
Cdd:cd03261   137 LSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHD-LDTAFAIADRIAVL 210

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065435   5 TQKQKmQRVDQVIQDLSLGKCQNTIIGvpgrvkGLSGGERKRLAFAsEAL-TDPPLLICDEPTSGLDSFMAASVVQVLKK 83
Cdd:COG1119   116 TDEQR-ERARELLELLGLAHLADRPFG------TLSQGEQRRVLIA-RALvKDPELLILDEPTAGLDLGARELLLALLDK 187

                          90       100       110
                  ....*....|....*....|....*....|
gi 1151065435  84 LSQRGKTVILTI-HQPsSELFELFDKILLM 112
Cdd:COG1119   188 LAAEGAPTLVLVtHHV-EEIPPGITHVLLL 216

Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065435  16 VIQDLSLGkcQNTIIGVpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTi 95
Cdd:cd03215    89 LVLDLSVA--ENIALSS-----LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLI- 160

                          90       100
                  ....*....|....*....|
gi 1151065435  96 hqpSSELFELF---DKILLM 112
Cdd:cd03215   161 ---SSELDELLglcDRILVM 177

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1151065435  27 NTIIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQrGKTVILTIHQP 98
Cdd:TIGR02868 462 DTVLGEGGAR--LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS-GRTVVLITHHL 530

nodulation factor ABC transporter ATP-binding protein NodI;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1151065435  35 RVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIH 96
Cdd:PRK13536  169 RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065435   4 MTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKK 83
Cdd:cd03264   102 IPSKEVKARVDEVLELVNLGDRAKK------KIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSE 175

                          90       100
                  ....*....|....*....|....*....
gi 1151065435  84 LSQrGKTVILTIHQpSSELFELFDKILLM 112
Cdd:cd03264   176 LGE-DRIVILSTHI-VEDVESLCNQVAVL 202

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065435  35 RVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQpSSELFELFDKILLM 112
Cdd:cd03268   123 KVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHL-LSEIQKVADRIGII 199

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065435  35 RVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKL-SQRGKTVILTIHQPssELF-ELFDKIL 110
Cdd:cd03256   141 RADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQV--DLArEYADRIV 216

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065435  30 IGVPGRvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSqRGKTVILTIHQPSseLFELFDKI 109
Cdd:cd03245   134 IGERGR--GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRI 208

                  ...
gi 1151065435 110 LLM 112
Cdd:cd03245   209 IVM 211