ID   CCMP_SYNY3              Reviewed;         213 AA.
AC   Q55550;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Carboxysome shell protein CcmP {ECO:0000305};
DE   AltName: Full=Carbon dioxide concentrating mechanism protein CcmP;
GN   Name=ccmP; OrderedLocusNames=slr0169;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- FUNCTION: Probably part of the carboxysome shell, a polyhedral
CC       inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS)
CC       is sequestered. It is thought that this protein controls transport of
CC       RuBisCO reactants in and out of the carboxysome.
CC       {ECO:0000250|UniProtKB:Q31QW7}.
CC   -!- SUBUNIT: A dimer of stacked trimers, the same faces interact.
CC       {ECO:0000250|UniProtKB:Q31QW7}.
CC   -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000250|UniProtKB:Q31QW7}.
CC       Note=This cyanobacterium makes beta-type carboxysomes. {ECO:0000305}.
CC   -!- DOMAIN: Contains 2 BMC domains, trimerizes to give a hexamer. Each
CC       trimer forms a pore with an opening of about 13 Angstroms in diameter;
CC       depending on the conformation of conserved residues Glu-69 and Arg-70
CC       the pore is open or closed. Dimerization of the trimers forms a small
CC       barrel-like compartment, accessible via the pore.
CC       {ECO:0000250|UniProtKB:Q31QW7}.
CC   -!- SIMILARITY: Belongs to the EutL/PduB family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01279}.
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DR   EMBL; BA000022; BAA10048.1; -; Genomic_DNA.
DR   PIR; S76070; S76070.
DR   AlphaFoldDB; Q55550; -.
DR   SMR; Q55550; -.
DR   IntAct; Q55550; 2.
DR   STRING; 1148.1001425; -.
DR   PaxDb; Q55550; -.
DR   EnsemblBacteria; BAA10048; BAA10048; BAA10048.
DR   KEGG; syn:slr0169; -.
DR   eggNOG; COG4577; Bacteria.
DR   InParanoid; Q55550; -.
DR   OMA; WIEVAPG; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0043886; F:structural constituent of carboxysome; IEA:UniProt.
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; -; 2.
DR   InterPro; IPR044870; BMC_CP.
DR   InterPro; IPR000249; BMC_dom.
DR   InterPro; IPR037233; CcmK-like_sf.
DR   SMART; SM00877; BMC; 2.
DR   SUPFAM; SSF143414; SSF143414; 1.
DR   PROSITE; PS51931; BMC_CP; 2.
PE   3: Inferred from homology;
KW   Bacterial microcompartment; Carbon dioxide fixation; Carboxysome;
KW   Photosynthesis; Reference proteome; Repeat.
FT   CHAIN           1..213
FT                   /note="Carboxysome shell protein CcmP"
FT                   /id="PRO_0000451247"
FT   DOMAIN          4..106
FT                   /note="BMC circularly permuted 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT   DOMAIN          107..206
FT                   /note="BMC circularly permuted 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01279"
FT   MOTIF           69..70
FT                   /note="Probably important for pore gating"
FT                   /evidence="ECO:0000250|UniProtKB:Q31QW7"
FT   SITE            18
FT                   /note="May bind RuBisCO reactants"
FT                   /evidence="ECO:0000250|UniProtKB:Q31QW7"
SQ   SEQUENCE   213 AA;  22745 MW;  EE12EF799038B2C6 CRC64;
     MGIELRSYVY LDSLQSQHAA YIGTVASGFL PLPGDCSLWV EVSPGIEINR ITDIALKAAV
     VRPGVLFVER LYGLLEIHAS NQGEVRAAGQ AILAYIGAKA SDCIKPKVVS SQIIRNIDAY
     QTQLINRNRR GHMLLAGQTL FVLEVQPAAY ASLAANEAEK SASINILQVS SIGSFGRLYL
     GGEERDIKAG ARAAIAAIEN APGKVPTLEG KNE