CCMO_SYNE7
ID CCMO_SYNE7 Reviewed; 276 AA.
AC P46205; Q31NB4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Carboxysome assembly protein CcmO {ECO:0000305};
DE AltName: Full=Carbon dioxide concentrating mechanism protein CcmO;
DE AltName: Full=ORF II {ECO:0000303|PubMed:2509426};
GN Name=ccmO {ECO:0000303|PubMed:16349207}; OrderedLocusNames=Synpcc7942_1425;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=2509426; DOI=10.1128/jb.171.11.6069-6076.1989;
RA Friedberg D., Kaplan A., Ariel R., Kessel M., Seijffers J.;
RT "The 5'-flanking region of the gene encoding the large subunit of ribulose-
RT 1,5-bisphosphate carboxylase/oxygenase is crucial for growth of the
RT cyanobacterium Synechococcus sp. strain PCC 7942 at the level of CO2 in
RT air.";
RL J. Bacteriol. 171:6069-6076(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=8491708; DOI=10.1128/jb.175.10.2871-2879.1993;
RA Price G.D., Howitt S.M., Harrison K., Badger M.R.;
RT "Analysis of a genomic DNA region from the cyanobacterium Synechococcus sp.
RT strain PCC7942 involved in carboxysome assembly and function.";
RL J. Bacteriol. 175:2871-2879(1993).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=16349207; DOI=10.1128/aem.60.3.1018-1020.1994;
RA Marco E., Martinez I., Ronen-Tarazi M., Orus M.I., Kaplan A.;
RT "Inactivation of ccmO in Synechococcus sp. Strain PCC 7942 Results in a
RT Mutant Requiring High Levels of CO(2).";
RL Appl. Environ. Microbiol. 60:1018-1020(1994).
RN [5]
RP FUNCTION, INTERACTION WITH CCMK2, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=22928045; DOI=10.1371/journal.pone.0043871;
RA Rae B.D., Long B.M., Badger M.R., Price G.D.;
RT "Structural determinants of the outer shell of beta-carboxysomes in
RT Synechococcus elongatus PCC 7942: roles for CcmK2, K3-K4, CcmO, and CcmL.";
RL PLoS ONE 7:e43871-e43871(2012).
RN [6]
RP CARBOXYSOME ASSEMBLY PROCESS, FUNCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=24267892; DOI=10.1016/j.cell.2013.10.044;
RA Cameron J.C., Wilson S.C., Bernstein S.L., Kerfeld C.A.;
RT "Biogenesis of a bacterial organelle: the carboxysome assembly pathway.";
RL Cell 155:1131-1140(2013).
RN [7]
RP BIOTECHNOLOGY.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=29922315; DOI=10.3389/fpls.2018.00739;
RA Fang Y., Huang F., Faulkner M., Jiang Q., Dykes G.F., Yang M., Liu L.N.;
RT "Engineering and Modulating Functional Cyanobacterial CO2-Fixing
RT Organelles.";
RL Front. Plant Sci. 9:739-739(2018).
RN [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=31048338; DOI=10.1105/tpc.18.00787;
RA Sun Y., Wollman A.J.M., Huang F., Leake M.C., Liu L.N.;
RT "Single-Organelle Quantification Reveals Stoichiometric and Structural
RT Variability of Carboxysomes Dependent on the Environment.";
RL Plant Cell 31:1648-1664(2019).
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 (PubMed:22928045, PubMed:24267892). Suggested to
CC be a carboxysome shell protein, but it is not detected in gels, mass
CC spectrometry or by protein sequencing (Probable).
CC {ECO:0000269|PubMed:22928045, ECO:0000269|PubMed:24267892,
CC ECO:0000305|PubMed:22928045, ECO:0000305|PubMed:24267892}.
CC -!- FUNCTION: Beta-carboxysome assembly initiates when soluble RuBisCO is
CC condensed into a liquid matrix in a pre-carboxysome by the RbcS-like
CC domains of probably both CcmM58 and CcmM35. CcmN interacts with the N-
CC terminus of CcmM58, and then recruits the CcmK2 major shell protein via
CC CcmN's encapsulation peptide. Shell formation requires CcmK proteins
CC and CcmO. CcmL caps the otherwise elongated carboxysome. Once fully
CC encapsulated carboxysomes are formed, they migrate within the cell
CC probably via interactions with the cytoskeleton.
CC {ECO:0000269|PubMed:24267892}.
CC -!- SUBUNIT: Homooligomerizes, possibly as a trimer, interacts with CcmK2
CC in the carboxysome. {ECO:0000269|PubMed:22928045}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:22928045,
CC ECO:0000269|PubMed:24267892, ECO:0000269|PubMed:31048338}. Note=This
CC cyanobacterium makes beta-type carboxysomes.
CC {ECO:0000269|PubMed:22928045}.
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:0000305|PubMed:22928045, ECO:0000305|PubMed:24267892}.
CC -!- DISRUPTION PHENOTYPE: Cells make aberrantly large polar bodies instead
CC of wild-type carboxysomes, do not grow in normal air but do grow on 4-
CC 5% CO(2), called a high-CO(2) requiring phenotype, HCR, no accumulation
CC of CcmK2 (PubMed:8491708, PubMed:22928045, PubMed:24267892). When ccmL-
CC ccmM-ccmN-ccmO are deleted no carboxysomes form, cells are HCR and
CC RuBisCO is soluble (PubMed:8491708). {ECO:0000269|PubMed:22928045,
CC ECO:0000269|PubMed:24267892, ECO:0000269|PubMed:8491708}.
CC -!- BIOTECHNOLOGY: Heterologous expression of 12 carboxysomal genes in
CC E.coli (ccaA, ccmK2, ccmK3, ccmK4, ccmL, ccmM, ccmN, ccmO, ccmP, rbcL,
CC rbcS, rbcX) leads to the formation of bodies that resemble
CC carboxysomes, have densely packed paracrystalline arrays and RuBisCO
CC activity. These structures open the door to generating carboxysomes in
CC plant cells to increase their photosynthesis and productivity, as well
CC as tailoring bacterial microcompartments to specific metabolic needs
CC and molecule delivery. {ECO:0000269|PubMed:29922315}.
CC -!- SIMILARITY: Belongs to the bacterial microcompartments protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU01278}.
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DR EMBL; M30808; AAA27327.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57455.1; -; Genomic_DNA.
DR RefSeq; WP_011242445.1; NC_007604.1.
DR AlphaFoldDB; P46205; -.
DR SMR; P46205; -.
DR STRING; 1140.Synpcc7942_1425; -.
DR PRIDE; P46205; -.
DR EnsemblBacteria; ABB57455; ABB57455; Synpcc7942_1425.
DR KEGG; syf:Synpcc7942_1425; -.
DR eggNOG; COG4577; Bacteria.
DR HOGENOM; CLU_078216_0_0_3; -.
DR OMA; CTAIVRG; -.
DR OrthoDB; 1802372at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1425-MON; -.
DR GO; GO:0031470; C:carboxysome; IDA:UniProtKB.
DR GO; GO:0043886; F:structural constituent of carboxysome; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Bacterial microcompartment; Carbon dioxide fixation; Carboxysome;
KW Photosynthesis; Repeat.
FT CHAIN 1..276
FT /note="Carboxysome assembly protein CcmO"
FT /id="PRO_0000004789"
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 35
FT /note="Missing (in Ref. 1; AAA27327)"
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
