ID K9PLZ2_9CYAN Unreviewed; 116 AA.
AC K9PLZ2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
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 ORFNames=Cal7507_3153 {ECO:0000313|EMBL:AFY33562.1};
OS Calothrix sp. PCC 7507.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY33562.1, ECO:0000313|Proteomes:UP000010390};
RN [1] {ECO:0000313|EMBL:AFY33562.1, ECO:0000313|Proteomes:UP000010390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY33562.1,
RC ECO:0000313|Proteomes:UP000010390};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A.,
RA Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA Woyke T., Kerfeld C.;
RT "Finished genome of Calothrix sp. PCC 7507.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003943; AFY33562.1; -; Genomic_DNA.
DR RefSeq; WP_015129371.1; NC_019682.1.
DR AlphaFoldDB; K9PLZ2; -.
DR STRING; 99598.Cal7507_3153; -.
DR KEGG; calo:Cal7507_3153; -.
DR PATRIC; fig|99598.3.peg.3578; -.
DR eggNOG; COG4577; Bacteria.
DR HOGENOM; CLU_064903_5_0_3; -.
DR OrthoDB; 7057533at2; -.
DR Proteomes; UP000010390; 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:UP000010390}.
FT DOMAIN 5..91
FT /note="BMC"
FT /evidence="ECO:0000259|PROSITE:PS51930"
SQ SEQUENCE 116 AA; 12330 MW; C1FE4C72EC6C851C CRC64;
MSLQAVGALE TKGFPAVLAA ADAMVKAGRV TLVGYIRVGS ARFTVNIRGD VSEVKTAMAA
GVEAAENVYG GTLESWVIIP RPHENVEAVL PIAYTEAVQQ YRESVENPII RSSNGR
//
