ID K9QTH0_NOSS7 Unreviewed; 116 AA.
AC K9QTH0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Carboxysome shell protein CcmK {ECO:0000256|HAMAP-Rule:MF_00854};
DE AltName: Full=Carbon dioxide-concentrating mechanism protein CcmK {ECO:0000256|HAMAP-Rule:MF_00854};
GN Name=ccmK {ECO:0000256|HAMAP-Rule:MF_00854};
GN OrderedLocusNames=Nos7524_2902 {ECO:0000313|EMBL:AFY48718.1};
OS Nostoc sp. (strain ATCC 29411 / PCC 7524).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=28072 {ECO:0000313|EMBL:AFY48718.1, ECO:0000313|Proteomes:UP000010378};
RN [1] {ECO:0000313|Proteomes:UP000010378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29411 / PCC 7524 {ECO:0000313|Proteomes:UP000010378};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- FUNCTION: One of the shell proteins of the carboxysome, a polyhedral
CC inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS)
CC is sequestered. Assembles into hexamers which make sheets that form the
CC facets of the polyhedral carboxysome. The hexamer central pore probably
CC regulates metabolite flux. {ECO:0000256|HAMAP-Rule:MF_00854}.
CC -!- SUBUNIT: Homohexamer. Interacts with CcmN and CcmO in the carboxysome.
CC {ECO:0000256|HAMAP-Rule:MF_00854}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000256|ARBA:ARBA00023587,
CC ECO:0000256|HAMAP-Rule:MF_00854}.
CC -!- DOMAIN: The tight homohexamer forms a small pore which is positively
CC charged. {ECO:0000256|HAMAP-Rule:MF_00854}.
CC -!- SIMILARITY: Belongs to the bacterial microcompartments protein family.
CC CcmK subfamily. {ECO:0000256|HAMAP-Rule:MF_00854}.
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DR EMBL; CP003552; AFY48718.1; -; Genomic_DNA.
DR RefSeq; WP_015139154.1; NC_019684.1.
DR AlphaFoldDB; K9QTH0; -.
DR STRING; 28072.Nos7524_2902; -.
DR KEGG; nop:Nos7524_2902; -.
DR PATRIC; fig|28072.8.peg.3176; -.
DR eggNOG; COG4577; Bacteria.
DR HOGENOM; CLU_064903_5_0_3; -.
DR OrthoDB; 7057533at2; -.
DR Proteomes; UP000010378; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0043886; F:structural constituent of carboxysome shell; IEA:UniProtKB-UniRule.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR CDD; cd07057; BMC_CcmK; 1.
DR Gene3D; 3.30.70.1710; -; 1.
DR HAMAP; MF_00854; CcmK; 1.
DR InterPro; IPR020808; Bact_microcomp_CS.
DR InterPro; IPR000249; BMC_dom.
DR InterPro; IPR046380; CcmK.
DR InterPro; IPR037233; CcmK-like_sf.
DR InterPro; IPR044872; CcmK/CsoS1_BMC.
DR PANTHER; PTHR33941:SF13; CARBOXYSOME SHELL PROTEIN CCMK4; 1.
DR PANTHER; PTHR33941; PROPANEDIOL UTILIZATION PROTEIN PDUA; 1.
DR Pfam; PF00936; BMC; 1.
DR SMART; SM00877; BMC; 1.
DR SUPFAM; SSF143414; CcmK-like; 1.
DR PROSITE; PS01139; BMC_1; 1.
DR PROSITE; PS51930; BMC_2; 1.
PE 3: Inferred from homology;
KW Bacterial microcompartment {ECO:0000256|ARBA:ARBA00024446};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW Rule:MF_00854}; Carboxysome {ECO:0000256|HAMAP-Rule:MF_00854};
KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00854};
KW Reference proteome {ECO:0000313|Proteomes:UP000010378}.
FT DOMAIN 5..91
FT /note="BMC"
FT /evidence="ECO:0000259|PROSITE:PS51930"
SQ SEQUENCE 116 AA; 12275 MW; 0AF5FC74371B000C CRC64;
MSLQAVGALE TKGFPAVLAA ADAMVKAGRV TLVGYIRVGS ARFTVNIRGD VSEVKTAMAA
GVEAAQNVHG GTLESWVIIP RPHENVEAVL PIGYTEAVQQ YRDSVENPII RSSNGR
//
