ID   CCMK1_THEVB             Reviewed;         113 AA.
AC   Q8DKB3;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Carboxysome shell protein CcmK1 {ECO:0000255|HAMAP-Rule:MF_00854, ECO:0000303|PubMed:22748766};
DE   AltName: Full=Carbon dioxide-concentrating mechanism protein CcmK1 {ECO:0000255|HAMAP-Rule:MF_00854};
GN   Name=ccmK1 {ECO:0000255|HAMAP-Rule:MF_00854, ECO:0000303|PubMed:22748766};
GN   OrderedLocusNames=tll0946;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
RN   [2] {ECO:0007744|PDB:3SSS}
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-102, SUBUNIT, AND DOMAIN.
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=22748766; DOI=10.1016/j.str.2012.05.013;
RA   Samborska B., Kimber M.S.;
RT   "A dodecameric CcmK2 structure suggests beta-carboxysomal shell facets have
RT   a double-layered organization.";
RL   Structure 20:1353-1362(2012).
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:0000255|HAMAP-Rule:MF_00854,
CC       ECO:0000305|PubMed:22748766}.
CC   -!- SUBUNIT: Homohexamer. Interacts preferentially with CcmK2 and CcmK4a
CC       rather than itself in vitro. {ECO:0000269|PubMed:22748766}.
CC   -!- INTERACTION:
CC       Q8DKB3; Q8DKB3: ccmK1; NbExp=2; IntAct=EBI-15992989, EBI-15992989;
CC       Q8DKB3; Q8DKB2: ccmK2; NbExp=2; IntAct=EBI-15992989, EBI-15992959;
CC   -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00854,
CC       ECO:0000305|PubMed:22748766}. Note=This cyanobacterium makes beta-type
CC       carboxysomes. {ECO:0000269|PubMed:22748766}.
CC   -!- DOMAIN: The tight homohexamer forms a small pore which is positively
CC       charged. {ECO:0000255|HAMAP-Rule:MF_00854,
CC       ECO:0000269|PubMed:22748766}.
CC   -!- SIMILARITY: Belongs to the bacterial microcompartments protein family.
CC       CcmK subfamily. {ECO:0000255|HAMAP-Rule:MF_00854}.
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DR   EMBL; BA000039; BAC08498.1; -; Genomic_DNA.
DR   RefSeq; NP_681736.1; NC_004113.1.
DR   RefSeq; WP_011056790.1; NC_004113.1.
DR   PDB; 3SSS; X-ray; 2.05 A; A/B/C/D/E/F=1-102.
DR   PDBsum; 3SSS; -.
DR   AlphaFoldDB; Q8DKB3; -.
DR   SMR; Q8DKB3; -.
DR   DIP; DIP-59853N; -.
DR   IntAct; Q8DKB3; 2.
DR   STRING; 197221.22294669; -.
DR   EnsemblBacteria; BAC08498; BAC08498; BAC08498.
DR   KEGG; tel:tll0946; -.
DR   PATRIC; fig|197221.4.peg.993; -.
DR   eggNOG; COG4577; Bacteria.
DR   OMA; QFREGVN; -.
DR   OrthoDB; 1802372at2; -.
DR   Proteomes; UP000000440; Chromosome.
DR   GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
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   Pfam; PF00936; BMC; 1.
DR   SMART; SM00877; BMC; 1.
DR   SUPFAM; SSF143414; SSF143414; 1.
DR   PROSITE; PS01139; BMC_1; 1.
DR   PROSITE; PS51930; BMC_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Bacterial microcompartment; Carbon dioxide fixation;
KW   Carboxysome; Photosynthesis; Reference proteome.
FT   CHAIN           1..113
FT                   /note="Carboxysome shell protein CcmK1"
FT                   /id="PRO_0000451239"
FT   DOMAIN          4..90
FT                   /note="BMC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00854"
FT   STRAND          4..12
FT                   /evidence="ECO:0007829|PDB:3SSS"
FT   HELIX           13..26
FT                   /evidence="ECO:0007829|PDB:3SSS"
FT   STRAND          30..36
FT                   /evidence="ECO:0007829|PDB:3SSS"
FT   STRAND          41..48
FT                   /evidence="ECO:0007829|PDB:3SSS"
FT   HELIX           50..64
FT                   /evidence="ECO:0007829|PDB:3SSS"
FT   STRAND          72..80
FT                   /evidence="ECO:0007829|PDB:3SSS"
FT   HELIX           83..87
FT                   /evidence="ECO:0007829|PDB:3SSS"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:3SSS"
FT   HELIX           98..101
FT                   /evidence="ECO:0007829|PDB:3SSS"
SQ   SEQUENCE   113 AA;  12059 MW;  AFB7C45988D7985E CRC64;
     MAIAVGMIET LGFPAVVEAA DAMVKAARVT LVGYEKIGSG RVTVIVRGDV SEVQASVAAG
     VENVKRVNGG QVLSTHIIAR PHENLEYVLP IRYTEAVEQF RESVSGIRPM GRP