CCMO_SYNP6
ID CCMO_SYNP6 Reviewed; 276 AA.
AC P23656; P23655; Q5N5U7;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Carboxysome assembly protein CcmO {ECO:0000305};
DE AltName: Full=Carbon dioxide concentrating mechanism protein CcmO;
GN Name=ccmO; OrderedLocusNames=syc0131_c;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Shinozaki K., Sugiura M.;
RT "Genes for the large and small subunits of ribulose-1,5-bisphosphate
RT carboxylase/oxygenase constitute a single operon in a cyanobacterium
RT Anacystis nidulans 6301.";
RL Mol. Gen. Genet. 200:27-32(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
CC -!- FUNCTION: Required for formation of the carboxysome, a polyhedral
CC inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS)
CC is sequestered. Required for recruitment of major shell protein CcmK2
CC to the pre-carboxysome. Suggested to be a carboxysome shell protein.
CC {ECO:0000250|UniProtKB:P46205}.
CC -!- SUBUNIT: Homooligomerizes, possibly as a trimer, interacts with CcmK in
CC the carboxysome. {ECO:0000250|UniProtKB:P46205}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000250|UniProtKB:P46205}.
CC Note=This cyanobacterium makes beta-type carboxysomes. {ECO:0000305}.
CC -!- DOMAIN: Has 2 BMC domains, is thought to trimerize giving a hexamer
CC that may interact with CcmK proteins in the carboxysome shell.
CC {ECO:0000250|UniProtKB:P46205}.
CC -!- SIMILARITY: Belongs to the bacterial microcompartments protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU01278}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA26970.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA26971.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X03220; CAA26970.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X03220; CAA26971.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AP008231; BAD78321.1; -; Genomic_DNA.
DR PIR; S07310; S07310.
DR RefSeq; WP_011242445.1; NC_006576.1.
DR AlphaFoldDB; P23656; -.
DR SMR; P23656; -.
DR STRING; 269084.syc0131_c; -.
DR EnsemblBacteria; BAD78321; BAD78321; syc0131_c.
DR KEGG; syc:syc0131_c; -.
DR eggNOG; COG4577; Bacteria.
DR OMA; CTAIVRG; -.
DR Proteomes; UP000001175; 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; IPR020808; Bact_microcomp_CS.
DR InterPro; IPR000249; BMC_dom.
DR InterPro; IPR037233; CcmK-like_sf.
DR InterPro; IPR044872; CcmK/CsoS1_BMC.
DR Pfam; PF00936; BMC; 2.
DR SMART; SM00877; BMC; 2.
DR SUPFAM; SSF143414; SSF143414; 2.
DR PROSITE; PS01139; BMC_1; 2.
DR PROSITE; PS51930; BMC_2; 2.
PE 3: Inferred from homology;
KW Bacterial microcompartment; Carbon dioxide fixation; Carboxysome;
KW Photosynthesis; Repeat.
FT CHAIN 1..276
FT /note="Carboxysome assembly protein CcmO"
FT /id="PRO_0000004788"
FT DOMAIN 16..100
FT /note="BMC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01278"
FT DOMAIN 120..204
FT /note="BMC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01278"
FT REGION 200..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 81
FT /note="Q -> T (in Ref. 1; CAA26970)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 276 AA; 29431 MW; F25514DB099D931F CRC64;
MSASLPAYSQ PRNAGALGVI CTRSFPAVVG TADMMLKSAD VTLIGYEKTG SGFCTAIIRG
GYADIKLALE AGVATARQFE QYVSSTILPR PQGNLEAVLP ISRRLSQEAM ATRSHQNVGA
IGLIETNGFP ALVGAADAML KSANVKLICY EKTGSGLCTA IVQGTVSNVT VAVEAGMYAA
ERIGQLNAIM VIPRPLDDLM DSLPEPQSDS EAAQPLQLPL RVREKQPLLE LPELERQPIA
IEAPRLLAEE RQSALELAQE TPLAEPLELP NPRDDQ