CCML_THEVB
ID CCML_THEVB Reviewed; 99 AA.
AC Q8DKB4;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=tll0945;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2] {ECO:0007744|PDB:4JVZ}
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS), SUBUNIT, AND DOMAIN.
RX PubMed=23949415; DOI=10.1007/s11120-013-9909-z;
RA Sutter M., Wilson S.C., Deutsch S., Kerfeld C.A.;
RT "Two new high-resolution crystal structures of carboxysome pentamer
RT proteins reveal high structural conservation of CcmL orthologs among
RT distantly related cyanobacterial species.";
RL Photosyn. Res. 118:9-16(2013).
RN [3] {ECO:0007744|PDB:4N8F}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), SUBUNIT, AND DOMAIN.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=24504539; DOI=10.1007/s11120-014-9973-z;
RA Keeling T.J., Samborska B., Demers R.W., Kimber M.S.;
RT "Interactions and structural variability of beta-carboxysomal shell protein
RT CcmL.";
RL Photosyn. Res. 121:125-133(2014).
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 -!- SUBUNIT: Homopentamer (PubMed:23949415, PubMed:24504539). May interact
CC with CcmK2, this occurs at very high CcmK2 concentrations (Probable).
CC Interacts with full-length CcmM (By similarity).
CC {ECO:0000250|UniProtKB:P72759, ECO:0000269|PubMed:23949415,
CC ECO:0000269|PubMed:24504539, ECO:0000305|PubMed:24504539}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000250|UniProtKB:Q03512,
CC ECO:0000255|HAMAP-Rule:MF_00858}. Note=This cyanobacterium makes beta-
CC type carboxysomes (Probable). Probably forms vertices in the
CC carboxysome (Probable). {ECO:0000305|PubMed:23949415}.
CC -!- DOMAIN: The tight homopentamer forms a pore with an opening of 4-5
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:0000255|HAMAP-Rule:MF_00858, ECO:0000269|PubMed:23949415,
CC ECO:0000269|PubMed:24504539}.
CC -!- SIMILARITY: Belongs to the CcmL/EutN family. CcmL subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00858}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000039; BAC08497.1; -; Genomic_DNA.
DR RefSeq; NP_681735.1; NC_004113.1.
DR RefSeq; WP_011056789.1; NC_004113.1.
DR PDB; 4JVZ; X-ray; 2.01 A; A/B/C/D/E=1-99.
DR PDB; 4N8F; X-ray; 2.00 A; A/B/C/D/E=1-99.
DR PDB; 7WKC; NMR; -; A/B/C/D/E=1-99.
DR PDBsum; 4JVZ; -.
DR PDBsum; 4N8F; -.
DR PDBsum; 7WKC; -.
DR AlphaFoldDB; Q8DKB4; -.
DR SMR; Q8DKB4; -.
DR STRING; 197221.22294668; -.
DR EnsemblBacteria; BAC08497; BAC08497; BAC08497.
DR KEGG; tel:tll0945; -.
DR PATRIC; fig|197221.4.peg.992; -.
DR eggNOG; COG4576; Bacteria.
DR OMA; GAGINEW; -.
DR OrthoDB; 1832681at2; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
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..99
FT /note="Carboxysome shell vertex protein CcmL"
FT /id="PRO_0000451291"
FT DOMAIN 1..83
FT /note="BMV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00858"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:4N8F"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:4N8F"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:4N8F"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:4N8F"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:4N8F"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:4N8F"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:4N8F"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:4N8F"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:4N8F"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:4N8F"
SQ SEQUENCE 99 AA; 10840 MW; 413705FED2E92958 CRC64;
MKIARVCGTV TSTQKEDTLT GVKFLVLQYL GEDGEFLPDY EVAADTVGAG QDEWVLVSRG
SAARHIINGT DKPIDAAVVA IIDTVSRDNY LLYSKRTQY
