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Database: UniProt
Entry: D7DVV4_NOSA0
LinkDB: D7DVV4_NOSA0
Original site: D7DVV4_NOSA0 
ID   D7DVV4_NOSA0            Unreviewed;       102 AA.
AC   D7DVV4;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 52.
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=Aazo_1865 {ECO:0000313|EMBL:ADI63963.1};
OS   Nostoc azollae (strain 0708) (Anabaena azollae (strain 0708)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Trichormus.
OX   NCBI_TaxID=551115 {ECO:0000313|EMBL:ADI63963.1, ECO:0000313|Proteomes:UP000001511};
RN   [1] {ECO:0000313|EMBL:ADI63963.1, ECO:0000313|Proteomes:UP000001511}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0708 {ECO:0000313|EMBL:ADI63963.1,
RC   ECO:0000313|Proteomes:UP000001511};
RX   PubMed=20628610; DOI=10.1371/journal.pone.0011486;
RA   Ran L., Larsson J., Vigil-Stenman T., Nylander J.A., Ininbergs K.,
RA   Zheng W.W., Lapidus A., Lowry S., Haselkorn R., Bergman B.;
RT   "Genome erosion in a nitrogen-fixing vertically transmitted endosymbiotic
RT   multicellular cyanobacterium.";
RL   PLoS ONE 5:E11486-E11486(2010).
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; CP002059; ADI63963.1; -; Genomic_DNA.
DR   RefSeq; WP_006276527.1; NC_014248.1.
DR   AlphaFoldDB; D7DVV4; -.
DR   STRING; 551115.Aazo_1865; -.
DR   GeneID; 67519726; -.
DR   KEGG; naz:Aazo_1865; -.
DR   eggNOG; COG4577; Bacteria.
DR   HOGENOM; CLU_064903_5_0_3; -.
DR   OrthoDB; 7057533at2; -.
DR   Proteomes; UP000001511; 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:UP000001511}.
FT   DOMAIN          4..90
FT                   /note="BMC"
FT                   /evidence="ECO:0000259|PROSITE:PS51930"
SQ   SEQUENCE   102 AA;  10920 MW;  C29298AD4DF5F3C1 CRC64;
     MPIAVGMIET KGFPAVVEAA DAMVKAARVT LVGYEKIGSA RVTVIVRGDV SEVQASVAAG
     IEAARRVNGG EVLSTHIIAR PHENLEYVLP IRYTEAVEQF RT
//
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