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Database: UniProt
Entry: G6FUV6_9CYAN
LinkDB: G6FUV6_9CYAN
Original site: G6FUV6_9CYAN 
ID   G6FUV6_9CYAN            Unreviewed;       114 AA.
AC   G6FUV6;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=FJSC11DRAFT_2653 {ECO:0000313|EMBL:EHC13036.1};
OS   Fischerella thermalis JSC-11.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC   Fischerella.
OX   NCBI_TaxID=741277 {ECO:0000313|EMBL:EHC13036.1, ECO:0000313|Proteomes:UP000004344};
RN   [1] {ECO:0000313|EMBL:EHC13036.1, ECO:0000313|Proteomes:UP000004344}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSC-11 {ECO:0000313|EMBL:EHC13036.1,
RC   ECO:0000313|Proteomes:UP000004344};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Sarkisova S., Bryant D.A., Brown I.,
RA   Woyke T.J.;
RT   "The draft genome of Fischerella sp. JSC-11.";
RL   Submitted (SEP-2011) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHC13036.1}.
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DR   EMBL; AGIZ01000007; EHC13036.1; -; Genomic_DNA.
DR   RefSeq; WP_009457332.1; NZ_AGIZ01000007.1.
DR   AlphaFoldDB; G6FUV6; -.
DR   GeneID; 60766722; -.
DR   PATRIC; fig|741277.3.peg.2211; -.
DR   Proteomes; UP000004344; Unassembled WGS sequence.
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:UP000004344}.
FT   DOMAIN          4..90
FT                   /note="BMC"
FT                   /evidence="ECO:0000259|PROSITE:PS51930"
SQ   SEQUENCE   114 AA;  12332 MW;  5199D14DC33C18B0 CRC64;
     MSIAVGMVET LGFPAVVEAA DAMVKAARVT LVGYEKIGSG RVTVIVRGDV SEVQASVAAG
     IESVKRVNGG QVLSTHIIAR PHENLEYVLP IRYTEDVEQF RENVNAIRPF GRRP
//
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