Carbon dioxide concentrating mechanism K (CcmK)-like proteins, Bacterial Micro-Compartment (BMC) domain; Bacterial micro-compartments are primitive protein-based organelles that sequester specific metabolic pathways in bacterial cells. The prototypical bacterial microcompartment is the carboxysome shell, a bacterial polyhedral organelle which increase the efficiency of CO2 fixation by encapsulating RuBisCO and carbonic anhydrase. They can be divided into two types: alpha-type carboxysomes (alpha-cyanobacteria and proteobacteria) and beta-type carboxysomes (beta-cyanobacteria). Potential functional differences between the two types are not yet fully understood. In addition to these proteins there are several homologous shell proteins including those found in pdu organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol and eut organelles involved in the cobalamin-dependent degradation of ethanolamine. Structure evidence shows that several carboxysome shell proteins and their homologs (Csos1A, CcmK1,2,4, and PduU) exist as hexamers which might further assemble into extended, tightly packed layers hypothesized to represent the flat facets of the polyhedral organelles outer shell. Although it has been suggested that other homologous proteins in this family might also form hexamers and play similar functional roles in the construction of their corresponding organelle outer shells at present no experimental evidence directly supports this view.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557372947   8 ALGAIETFGLVWVLEAGDAMCKAGDVRLIGYENTASGYISILVEGDVAACEAAVTAGVKAVEALGaEVYSSVVIARPHPS 87
Cdd:cd07045     1 ALGLIETRGLVAAIEAADAALKAANVTLVGYEKVGGGLVTVKITGDVAAVKAAVEAGAAAAERIG-ELVSSHVIPRPHDE 79

                  ....
gi 2557372947  88 LKKI 91
Cdd:cd07045    80 VEKI 83

Bacterial microcompartments are primitive organelles composed entirely of protein subunits; The prototypical bacterial microcompartment is the carboxysome, a protein shell for sequestering carbon fixation reactions. These proteins for hexameric structure.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2557372947    8 ALGAIETFGLVWVLEAGDAMCKAGDVRLIGYENTASGYISILVEGDVAACEAAVTAGVKAVEALGaeVYSSVVIARP 84
Cdd:smart00877   1 ALGIIETRGAAAAIEAADAALKAANVELVGYESIGGGKVTVIITGDVAAVRAAVEAGLEAAERLG--LVSSHVIPRP 75

Carbon dioxide concentrating mechanism K (CcmK)-like proteins, Bacterial Micro-Compartment (BMC) domain; Bacterial micro-compartments are primitive protein-based organelles that sequester specific metabolic pathways in bacterial cells. The prototypical bacterial microcompartment is the carboxysome shell, a bacterial polyhedral organelle which increase the efficiency of CO2 fixation by encapsulating RuBisCO and carbonic anhydrase. They can be divided into two types: alpha-type carboxysomes (alpha-cyanobacteria and proteobacteria) and beta-type carboxysomes (beta-cyanobacteria). Potential functional differences between the two types are not yet fully understood. In addition to these proteins there are several homologous shell proteins including those found in pdu organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol and eut organelles involved in the cobalamin-dependent degradation of ethanolamine. Structure evidence shows that several carboxysome shell proteins and their homologs (Csos1A, CcmK1,2,4, and PduU) exist as hexamers which might further assemble into extended, tightly packed layers hypothesized to represent the flat facets of the polyhedral organelles outer shell. Although it has been suggested that other homologous proteins in this family might also form hexamers and play similar functional roles in the construction of their corresponding organelle outer shells at present no experimental evidence directly supports this view.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557372947   8 ALGAIETFGLVWVLEAGDAMCKAGDVRLIGYENTASGYISILVEGDVAACEAAVTAGVKAVEALGaEVYSSVVIARPHPS 87
Cdd:cd07045     1 ALGLIETRGLVAAIEAADAALKAANVTLVGYEKVGGGLVTVKITGDVAAVKAAVEAGAAAAERIG-ELVSSHVIPRPHDE 79

                  ....
gi 2557372947  88 LKKI 91
Cdd:cd07045    80 VEKI 83

BMC domain; Bacterial microcompartments are primitive organelles composed entirely of protein subunits. The prototypical bacterial microcompartment is the carboxysome, a protein shell for sequestering carbon fixation reactions. These proteins for hexameric structure.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2557372947   8 ALGAIETFGLVWVLEAGDAMCKAGDVRLIGYENTASGYISILVEGDVAACEAAVTAGVKAVEALGaEVYSSVVIA 82
Cdd:pfam00936   1 ALGLIETRGLAAGIEAADAMLKAANVELVGYELIGGGKVTVIITGDVAAVKAAVEAGVEAAERIG-ELVSSHVIP 74

Carboxysome Shell 1 (CsoS1); Bacterial Micro-Compartment (BMC) domain; The cso operon in Halothiobacillus neapolitanus contains the genes involved in alpha carboxysome function including those for the carboxysome shell proteins: CsoS1A, CsoS1B, and CsoS1C. CsoS1A has been shown to form hexameric units which further assemble into the flat facets of the polyhedral carboxysome shell. The structures suggest that the central pores and the gaps between hexamers limit the transport of metabolites into and out of the the carboxysome. Although it has been suggested that other homologous proteins, CsoS1B and CsoS1C, in this family might also form hexamers and play similar functional roles in the construction of carboxysome outer shell at present no experimental evidence directly supports this view.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557372947   8 ALGAIETFGLVWVLEAGDAMCKAGDVRLIGYENTASGYISILVEGDVAACEAAVTAGVKAVEALGAEVYSSVVIARPHPS 87
Cdd:cd07058     3 ALGMIETRGLVPAIEAADAMTKAAEVRLIGRQFVGGGYVTVLVRGETGAVNAAVRAGADACERVGDGLVAAHIIARVHSE 82

                  ....
gi 2557372947  88 LKKI 91
Cdd:cd07058    83 VENI 86

ethanolamine utilization microcompartment protein EutK;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2557372947   6 MNALGAIETFGLVWVLEAGDAMCKAGDVRLIGYENTASGYISILVEGDVAACEAAVTAGVKAVEALGaEVYSSVVIARP 84
Cdd:PRK15466    2 INALGLLEVDGMVAAIDAADAMLKAANVRLLSHEVLDPGRLTLVVEGDLAACRAALDAGCAAAMRTG-RVISRKEIGRP 79

1,2-propanediol utilization protein K (PduK), Bacterial Micro-Compartment (BMC) domain repeat 1l; PduK proteins are homologs of the carboxysome shell protein. They are encoded within the pdu operon and might be required for the formation of the outer shell of the bacterial pdu polyhedral organelles which are involved in coenzyme B12-dependent degradation of 1,2-propanediol. Although it has been suggested that PduK might form hexamers and further assemble into the flat facets of the polyhedral outer shell of pdu organelles at present no experimental evidence directly supports this view.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2557372947   8 ALGAIETFGLVWVLEAGDAMCKAGDVRLIGYENT-ASGYISILVEGDVAACEAAVTAGVKAVEALGAEVySSVVIARP 84
Cdd:cd07056     1 SLGLLEVSGLSGAIVVADRMAKTANVRLLGLENTkGSGWMTVKISGDVAAVNAAIEAGKQTAGASDGYV-ASTVIARP 77

Bacterial Micro-Compartment (BMC) domain; Bacterial micro-compartments are primitive protein-based organelles that sequester specific metabolic pathways in bacterial cells. The prototypical bacterial microcompartment is the carboxysome shell, a bacterial polyhedral organelle which increase the efficiency of CO2 fixation by encapsulating RuBisCO and carbonic anhydrase. They can be divided into two types: alpha-type carboxysomes (alpha-cyanobacteria and proteobacteria) and beta-type carboxysomes (beta-cyanobacteria). In addition to these proteins there are several homologous shell proteins including those found in pdu organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol and eut organelles involved in the cobalamin-dependent degradation of ethanolamine. Structure evidence shows that several carboxysome shell proteins and their homologs (Csos1A, CcmK1,2,4, and PduU) exist as hexamers which might further assemble into extended, tightly packed layers hypothesized to represent the flat facets of the polyhedral organelles outer shell. Although it has been suggested that other homologous proteins in this family might also form hexamers and play similar functional roles in the construction of their corresponding organelle outer shell at present no experimental evidence directly supports this view.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2557372947   8 ALGAIETFGLVWVLEAGDAMCKAGDVRLIGYENTA-SGYISILVEGDVAACEAAVTAGVKA 67
Cdd:cd06169     1 ALGLLEVRGLAAAIVAADAAVKAADVELVGIERAGgGGLVTLIIRGDVSAVKAAVEAAEQA 61