CCML_SYNE7
ID CCML_SYNE7 Reviewed; 99 AA.
AC Q03512; Q31NB7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Carboxysome shell vertex protein CcmL {ECO:0000255|HAMAP-Rule:MF_00858};
DE AltName: Full=Carbon dioxide concentrating mechanism protein CcmL {ECO:0000255|HAMAP-Rule:MF_00858};
GN Name=ccmL {ECO:0000255|HAMAP-Rule:MF_00858, ECO:0000303|PubMed:8491708};
GN OrderedLocusNames=Synpcc7942_1422;
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], AND 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 [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 CARBOXYSOME ASSEMBLY PROCESS, FUNCTION, AND 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 [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=28616951; DOI=10.1039/c7nr02524f;
RA Faulkner M., Rodriguez-Ramos J., Dykes G.F., Owen S.V., Casella S.,
RA Simpson D.M., Beynon R.J., Liu L.N.;
RT "Direct characterization of the native structure and mechanics of
RT cyanobacterial carboxysomes.";
RL Nanoscale 9:10662-10673(2017).
RN [5]
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 [6]
RP SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION.
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: Probably forms vertices in the carboxysome, a polyhedral
CC inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS)
CC is sequestered. Has been modeled to induce curvature upon insertion
CC into an otherwise flat hexagonal molecular layer of CcmK subunits.
CC {ECO:0000250|UniProtKB:P72759, ECO:0000255|HAMAP-Rule:MF_00858,
CC 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: Homopentamer (Probable). Interacts with full-length CcmM (By
CC similarity). {ECO:0000250|UniProtKB:P72759,
CC ECO:0000305|PubMed:31048338}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00858,
CC ECO:0000269|PubMed:28616951, ECO:0000269|PubMed:31048338}. Note=This
CC cyanobacterium makes beta-type carboxysomes (PubMed:24267892). Probably
CC forms vertices in the polyhedral carboxysome (Probable).
CC {ECO:0000269|PubMed:24267892, ECO:0000305|PubMed:24267892}.
CC -!- INDUCTION: Carboxysome size and components vary with growth conditions.
CC When grown in ambient air at medium light (50 uE meter(-2) second(-1))
CC there are 7.4 units of this protein per carboxysome, the numbers are
CC stable under low light, and increase under high light and high CO(2)
CC (at protein level). {ECO:0000269|PubMed:31048338}.
CC -!- DOMAIN: The tight homopentamer forms a pore with an opening of about 5
CC Angstroms in diameter which opens into a wider tunnel at the base of
CC the truncated pyramid. The pore is positively charged.
CC {ECO:0000250|UniProtKB:P72759}.
CC -!- DISRUPTION PHENOTYPE: An insertion in this gene leads to rod-shaped
CC carboxysomes and an inability to grow in normal air, called a high-
CC CO(2) requiring phenotype, HCR. When ccmL-ccmM-ccmN-ccmO are deleted no
CC carboxysomes form, cells are HCR and RuBisCO is soluble. Both mutants
CC grow on 2% CO(2). {ECO:0000269|PubMed:24267892,
CC 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 CcmL/EutN family. CcmL subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00858}.
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DR EMBL; M96929; AAA27305.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57452.1; -; Genomic_DNA.
DR PIR; C36904; C36904.
DR RefSeq; WP_011242448.1; NC_007604.1.
DR AlphaFoldDB; Q03512; -.
DR SMR; Q03512; -.
DR STRING; 1140.Synpcc7942_1422; -.
DR PRIDE; Q03512; -.
DR EnsemblBacteria; ABB57452; ABB57452; Synpcc7942_1422.
DR KEGG; syf:Synpcc7942_1422; -.
DR eggNOG; COG4576; Bacteria.
DR HOGENOM; CLU_148498_0_1_3; -.
DR OMA; GAGINEW; -.
DR OrthoDB; 1832681at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1422-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 CDD; cd01614; EutN_CcmL; 1.
DR Gene3D; 2.40.50.220; -; 1.
DR HAMAP; MF_00858; CcmL; 1.
DR InterPro; IPR046387; CcmL.
DR InterPro; IPR004992; EutN_CcmL.
DR InterPro; IPR036677; EutN_CcmL_sf.
DR PANTHER; PTHR36539; PTHR36539; 1.
DR Pfam; PF03319; EutN_CcmL; 1.
DR SUPFAM; SSF159133; SSF159133; 1.
DR PROSITE; PS51932; BMV; 1.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; Carbon dioxide fixation; Carboxysome;
KW Photosynthesis.
FT CHAIN 1..99
FT /note="Carboxysome shell vertex protein CcmL"
FT /id="PRO_0000089426"
FT DOMAIN 1..83
FT /note="BMV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00858"
SQ SEQUENCE 99 AA; 11016 MW; BEB981074B435460 CRC64;
MRIAKVRGTV VSTYKEPSLQ GVKFLVVQFL DEAGQALQEY EVAADMVGAG VDEWVLISRG
SQARHVRDCQ ERPVDAAVIA IIDTVNVENR SVYDKREHS
