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CH604_RHIME
ID   CH604_RHIME             Reviewed;         545 AA.
AC   Q92ZQ4;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Chaperonin GroEL 4 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=60 kDa chaperonin 4 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=Chaperonin-60 4 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            Short=Cpn60 4 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Name=groEL4 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=groL4 {ECO:0000255|HAMAP-Rule:MF_00600}; OrderedLocusNames=RA0395;
GN   ORFNames=SMa0744;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OG   Plasmid pSymA (megaplasmid 1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481432; DOI=10.1073/pnas.161294798;
RA   Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F.,
RA   Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA   Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA   Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA   Long S.R.;
RT   "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT   meliloti pSymA megaplasmid.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
CC   -!- FUNCTION: Together with its co-chaperonin GroES, plays an essential
CC       role in assisting protein folding. The GroEL-GroES system forms a nano-
CC       cage that allows encapsulation of the non-native substrate proteins and
CC       provides a physical environment optimized to promote and accelerate
CC       protein folding. {ECO:0000255|HAMAP-Rule:MF_00600}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an
CC         unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00600};
CC   -!- SUBUNIT: Forms a cylinder of 14 subunits composed of two heptameric
CC       rings stacked back-to-back. Interacts with the co-chaperonin GroES.
CC       {ECO:0000255|HAMAP-Rule:MF_00600}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC       {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR   EMBL; AE006469; AAK65053.1; -; Genomic_DNA.
DR   PIR; C95311; C95311.
DR   RefSeq; NP_435641.1; NC_003037.1.
DR   RefSeq; WP_010967384.1; NC_003037.1.
DR   AlphaFoldDB; Q92ZQ4; -.
DR   SMR; Q92ZQ4; -.
DR   EnsemblBacteria; AAK65053; AAK65053; SMa0744.
DR   GeneID; 25012147; -.
DR   GeneID; 61599213; -.
DR   KEGG; sme:SMa0744; -.
DR   PATRIC; fig|266834.11.peg.411; -.
DR   HOGENOM; CLU_016503_3_0_5; -.
DR   OMA; TGAQLMR; -.
DR   PRO; PR:Q92ZQ4; -.
DR   Proteomes; UP000001976; Plasmid pSymA.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   CDD; cd03344; GroEL; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   HAMAP; MF_00600; CH60; 1.
DR   InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR   InterPro; IPR001844; Cpn60/GroEL.
DR   InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR   InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   InterPro; IPR027410; TCP-1-like_intermed_sf.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00298; CHAPERONIN60.
DR   SUPFAM; SSF48592; SSF48592; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 1.
DR   TIGRFAMs; TIGR02348; GroEL; 1.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding; Plasmid;
KW   Reference proteome; Stress response.
FT   CHAIN           1..545
FT                   /note="Chaperonin GroEL 4"
FT                   /id="PRO_0000063503"
FT   BINDING         30..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         87..91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         415
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         495
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   545 AA;  57701 MW;  49BA61F23CE70431 CRC64;
     MAAKEVKFGR SAREKMLRGV DILADAVKVT LGPKGRNVVI DKSFGAPRIT KDGVTVAKEI
     ELEDKFENMG AQMVREVASK TNDIAGDGTT TATVLAQAIV REGAKAVAAG MNPMDLKRGI
     DLAVAEVVKD LLAKAKKINT SDEVAQVGTI SANGEKQIGL DIAEAMQKVG NEGVITVEEA
     KTAETELEVV EGMQFDRGYL SPYFVTNPEK MVADLEDAFI LLHEKKLSNL QAMLPVLEAV
     VQTGKPLLII AEDVEGEALA TLVVNKLRGG LKIAAVKAPG FGDRRKAMLE DIAILTGGTV
     ISEDLGIKLE SVTLDMLGRA KKVSITKENT TIVDGAGQKS DIEGRVAQIK AQIEETTSDY
     DREKLQERLA KLAGGVAVIR VGGATEVEVK EKKDRIDDAL NATRAAVQEG IVPGGGVALL
     RSSVKITVKG ENDDQDAGVN IVRRALQSPA RQIVENAGDE ASIVVGKILE KNTDDFGYNA
     QTGEYGDMIA MGIIDPVKVV RTALQDAASV ASLLITTEAM IAELPKKDAP AMPGGMGGMG
     GMDMM
 
 
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