CCML_SYNY3
ID CCML_SYNY3 Reviewed; 100 AA.
AC P72759;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 104.
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}; OrderedLocusNames=sll1030;
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).
RN [2]
RP INTERACTION WITH CCMM.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=17993516; DOI=10.1128/jb.01283-07;
RA Cot S.S., So A.K., Espie G.S.;
RT "A multiprotein bicarbonate dehydration complex essential to carboxysome
RT function in cyanobacteria.";
RL J. Bacteriol. 190:936-945(2008).
RN [3] {ECO:0007744|PDB:2QW7}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND DOMAIN.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=18292340; DOI=10.1126/science.1151458;
RA Tanaka S., Kerfeld C.A., Sawaya M.R., Cai F., Heinhorst S., Cannon G.C.,
RA Yeates T.O.;
RT "Atomic-level models of the bacterial carboxysome shell.";
RL Science 319:1083-1086(2008).
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:0000255|HAMAP-Rule:MF_00858, ECO:0000305|PubMed:18292340}.
CC -!- SUBUNIT: Homopentamer (PubMed:18292340). Interacts with full-length
CC CcmM (PubMed:17993516). {ECO:0000255|HAMAP-Rule:MF_00858,
CC ECO:0000269|PubMed:17993516, ECO:0000269|PubMed:18292340}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00858,
CC ECO:0000305|PubMed:18292340}. Note=This cyanobacterium makes beta-type
CC carboxysomes (Probable). Probably forms vertices in the polyhedral
CC carboxysome (Probable). {ECO:0000305|PubMed:17993516,
CC ECO:0000305|PubMed:18292340}.
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:0000269|PubMed:18292340}.
CC -!- SIMILARITY: Belongs to the CcmL/EutN family. CcmL subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00858}.
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DR EMBL; BA000022; BAA16774.1; -; Genomic_DNA.
DR PIR; S74622; S74622.
DR PDB; 2QW7; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J=1-100.
DR PDBsum; 2QW7; -.
DR AlphaFoldDB; P72759; -.
DR SMR; P72759; -.
DR IntAct; P72759; 5.
DR STRING; 1148.1651847; -.
DR PaxDb; P72759; -.
DR EnsemblBacteria; BAA16774; BAA16774; BAA16774.
DR KEGG; syn:sll1030; -.
DR eggNOG; COG4576; Bacteria.
DR InParanoid; P72759; -.
DR OMA; GAGINEW; -.
DR PhylomeDB; P72759; -.
DR EvolutionaryTrace; P72759; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0043886; F:structural constituent of carboxysome; IPI: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 3D-structure; Bacterial microcompartment; Carbon dioxide fixation;
KW Carboxysome; Photosynthesis; Reference proteome.
FT CHAIN 1..100
FT /note="Carboxysome shell vertex protein CcmL"
FT /id="PRO_0000089427"
FT DOMAIN 1..83
FT /note="BMV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00858"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:2QW7"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:2QW7"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:2QW7"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:2QW7"
FT STRAND 36..47
FT /evidence="ECO:0007829|PDB:2QW7"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:2QW7"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:2QW7"
FT STRAND 75..86
FT /evidence="ECO:0007829|PDB:2QW7"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:2QW7"
SQ SEQUENCE 100 AA; 10638 MW; 745B80ED084E7680 CRC64;
MQLAKVLGTV VSTSKTPNLT GVKLLLVQFL DTKGQPLERY EVAGDVVGAG LNEWVLVARG
SAARKERGNG DRPLDAMVVG IIDTVNVASG SLYNKRDDGR
