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CH10_CHLMU
ID   CH10_CHLMU              Reviewed;         102 AA.
AC   P17204;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Co-chaperonin GroES {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=10 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=11.2 kDa stress response protein;
DE   AltName: Full=Chaperonin-10 {ECO:0000255|HAMAP-Rule:MF_00580};
DE            Short=Cpn10 {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=Heat shock protein 10;
DE            Short=HSP10;
GN   Name=groES {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Synonyms=groS {ECO:0000255|HAMAP-Rule:MF_00580}, hypA, mopB;
GN   OrderedLocusNames=TC_0387;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MoPn;
RX   PubMed=7909303; DOI=10.1016/0378-1119(94)90145-7;
RA   Ho Y., Zhang Y.-X.;
RT   "The sequence of the groES and groEL genes from the mouse pneumonitis agent
RT   of Chlamydia trachomatis.";
RL   Gene 141:143-144(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MoPn;
RX   PubMed=8955323; DOI=10.1128/jb.178.23.6983-6990.1996;
RA   Tan M., Wong B., Engel J.N.;
RT   "Transcriptional organization and regulation of the dnaK and groE operons
RT   of Chlamydia trachomatis.";
RL   J. Bacteriol. 178:6983-6990(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
CC   -!- FUNCTION: Together with the chaperonin GroEL, plays an essential role
CC       in assisting protein folding. The GroEL-GroES system forms a nano-cage
CC       that allows encapsulation of the non-native substrate proteins and
CC       provides a physical environment optimized to promote and accelerate
CC       protein folding. GroES binds to the apical surface of the GroEL ring,
CC       thereby capping the opening of the GroEL channel. {ECO:0000255|HAMAP-
CC       Rule:MF_00580}.
CC   -!- SUBUNIT: Heptamer of 7 subunits arranged in a ring. Interacts with the
CC       chaperonin GroEL. {ECO:0000255|HAMAP-Rule:MF_00580}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00580}.
CC   -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000255|HAMAP-
CC       Rule:MF_00580, ECO:0000305}.
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DR   EMBL; L12004; AAA19870.1; -; Genomic_DNA.
DR   EMBL; U52049; AAA97910.1; -; Genomic_DNA.
DR   EMBL; AE002160; AAF39244.1; -; Genomic_DNA.
DR   PIR; E81709; E81709.
DR   RefSeq; WP_009872382.1; NZ_CP027217.1.
DR   AlphaFoldDB; P17204; -.
DR   SMR; P17204; -.
DR   STRING; 243161.TC_0387; -.
DR   EnsemblBacteria; AAF39244; AAF39244; TC_0387.
DR   GeneID; 66303432; -.
DR   KEGG; cmu:TC_0387; -.
DR   eggNOG; COG0234; Bacteria.
DR   HOGENOM; CLU_132825_2_1_0; -.
DR   OMA; EVKYSGE; -.
DR   OrthoDB; 1965002at2; -.
DR   Proteomes; UP000000800; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd00320; cpn10; 1.
DR   Gene3D; 2.30.33.40; -; 1.
DR   HAMAP; MF_00580; CH10; 1.
DR   InterPro; IPR020818; Chaperonin_GroES.
DR   InterPro; IPR037124; Chaperonin_GroES_sf.
DR   InterPro; IPR018369; Chaprnonin_Cpn10_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   PANTHER; PTHR10772; PTHR10772; 1.
DR   Pfam; PF00166; Cpn10; 1.
DR   PRINTS; PR00297; CHAPERONIN10.
DR   SMART; SM00883; Cpn10; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   PROSITE; PS00681; CHAPERONINS_CPN10; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Stress response.
FT   CHAIN           1..102
FT                   /note="Co-chaperonin GroES"
FT                   /id="PRO_0000174727"
SQ   SEQUENCE   102 AA;  11183 MW;  19961A370F903AB6 CRC64;
     MSDQATTLKI KPLGDRILVK REEEASTARG GIILPDTAKK KQDRAEVLAL GTGKKDDKGQ
     QLPFEVQVGD IVLIDKYSGQ ELTVEGEEYV IVQMSEVIAV LQ
 
 
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