ID A0A0C2KRY5_9CYAN Unreviewed; 115 AA.
AC A0A0C2KRY5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=SD81_28105 {ECO:0000313|EMBL:KIJ73367.1};
OS Tolypothrix campylonemoides VB511288.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ73367.1};
RN [1] {ECO:0000313|EMBL:KIJ73367.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB511288 {ECO:0000313|EMBL:KIJ73367.1};
RA Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT VB511288.";
RL Submitted (JAN-2015) 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:KIJ73367.1}.
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DR EMBL; JXCB01000012; KIJ73367.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2KRY5; -.
DR OrthoDB; 7057533at2; -.
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}.
FT DOMAIN 4..90
FT /note="BMC"
FT /evidence="ECO:0000259|PROSITE:PS51930"
SQ SEQUENCE 115 AA; 12419 MW; 3C4BE3A118FB8876 CRC64;
MSIAVGMVET LGFPAVVEAA DAMVKAARVT LVGYEKIGSG RVTVIVRGDV SEVQASVGAG
VESVKRVNGG QVLSTHIIAR PHENLEYVLP IRYTEDVEQF RENVNAITRP YNPRP
//
