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Database: UniProt
Entry: K9YHS7_HALP7
LinkDB: K9YHS7_HALP7
Original site: K9YHS7_HALP7 
ID   K9YHS7_HALP7            Unreviewed;       113 AA.
AC   K9YHS7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=PCC7418_3532 {ECO:0000313|EMBL:AFZ45643.1};
OS   Halothece sp. (strain PCC 7418) (Synechococcus sp. (strain PCC 7418)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Halothecacae; Halothece cluster; Halothece.
OX   NCBI_TaxID=65093 {ECO:0000313|EMBL:AFZ45643.1, ECO:0000313|Proteomes:UP000010481};
RN   [1] {ECO:0000313|Proteomes:UP000010481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7418 {ECO:0000313|Proteomes:UP000010481};
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).
RN   [2] {ECO:0007829|PDB:6OWF, ECO:0007829|PDB:6OWG}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.60 ANGSTROMS).
RX   PubMed=31501298; DOI=10.1104/pp.19.00885;
RA   Sutter M., Laughlin T.G., Sloan N.B., Serwas D., Davies K.M., Kerfeld C.A.;
RT   "Structure of a Synthetic <i>beta</i>-Carboxysome Shell.";
RL   Plant Physiol. 181:1050-1058(2019).
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; CP003945; AFZ45643.1; -; Genomic_DNA.
DR   RefSeq; WP_015227515.1; NC_019779.1.
DR   PDB; 6OWF; EM; 3.00 A; 1/2/4/5/7/8/A/A0/A2/A3/A5/A6/A8/A9/AB/AC/AE/AF/AH/AI/AK/AL/AN/AO/AQ/AR/AT/AU/AW/AX=1-113.
DR   PDB; 6OWG; EM; 2.60 A; 0/2/3/4/6/7/8/A/A0/A1/A2/A4/A5/A6/A8/A9/AA/AC/AD/AE/AG/AH/AI/AK/AL/AM/AO/AP/AQ/AS=1-113.
DR   PDBsum; 6OWF; -.
DR   PDBsum; 6OWG; -.
DR   AlphaFoldDB; K9YHS7; -.
DR   SMR; K9YHS7; -.
DR   STRING; 65093.PCC7418_3532; -.
DR   KEGG; hao:PCC7418_3532; -.
DR   PATRIC; fig|65093.3.peg.3735; -.
DR   eggNOG; COG4577; Bacteria.
DR   HOGENOM; CLU_064903_5_0_3; -.
DR   OrthoDB; 7057533at2; -.
DR   Proteomes; UP000010481; 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; 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; PS51930; BMC_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:6OWF, ECO:0007829|PDB:6OWG};
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:UP000010481}.
FT   DOMAIN          4..90
FT                   /note="BMC"
FT                   /evidence="ECO:0000259|PROSITE:PS51930"
SQ   SEQUENCE   113 AA;  12150 MW;  C69FCCF494741D5A CRC64;
     MAVAVGMIET LGFPAVVEAA DAMVKAARVT LVGYEKIGTG RVTVIVRGDV SEVQASVSAG
     TESVKRVNGG QVLSTHIIAR PHENLEYVLP IRYTEEVEQF REGVGTPRNI TRQ
//
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