CH602_RHIME
ID CH602_RHIME Reviewed; 542 AA.
AC P35470;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Chaperonin GroEL 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL2 {ECO:0000255|HAMAP-Rule:MF_00600}; OrderedLocusNames=R01196;
GN ORFNames=SMc01758;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=8097179; DOI=10.1016/0378-1119(93)90591-p;
RA Rusanganwa E., Gupta R.S.;
RT "Cloning and characterization of multiple groEL chaperonin-encoding genes
RT in Rhizobium meliloti.";
RL Gene 126:67-75(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
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 -!- INDUCTION: By heat shock.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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; M94190; AAA26283.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC45775.1; -; Genomic_DNA.
DR PIR; JN0511; JN0511.
DR RefSeq; NP_385302.1; NC_003047.1.
DR RefSeq; WP_003529335.1; NC_003047.1.
DR AlphaFoldDB; P35470; -.
DR SMR; P35470; -.
DR STRING; 266834.SMc01758; -.
DR EnsemblBacteria; CAC45775; CAC45775; SMc01758.
DR GeneID; 61602654; -.
DR KEGG; sme:SMc01758; -.
DR PATRIC; fig|266834.11.peg.2607; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_5; -.
DR OMA; GSETFGF; -.
DR Proteomes; UP000001976; Chromosome.
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 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW Reference proteome; Stress response.
FT CHAIN 1..542
FT /note="Chaperonin GroEL 2"
FT /id="PRO_0000063501"
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 496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 269..270
FT /note="GG -> AS (in Ref. 1; AAA26283)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="G -> R (in Ref. 1; AAA26283)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="R -> P (in Ref. 1; AAA26283)"
FT /evidence="ECO:0000305"
FT CONFLICT 503..505
FT /note="AAL -> TAV (in Ref. 1; AAA26283)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="Missing (in Ref. 1; AAA26283)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 57984 MW; DAA2F493C3A70A1D CRC64;
MAAKEVKFTS DARDRMLRGV DIMANAVRVT LGPKGRNVVI DKSFGAPRIT KDGVSVAKEI
ELEDKFENMG AQMLREVASR TSDIAGDGTT TATVLAQAIV REGAKAVASG MNPMDLKRGI
DLAVEAIVKE LRNNARKVSK NAEIAQVATI SANGDAEIGR YLAEAMEKVG NEGVITVEEA
KTAEIELEVV EGMEFDRGYL SPYFITNQEK MRVELEDAYI LLHEKKLSNL QAMIPILESV
IQSGKPLLII AEDVEGEALA TLVVNKLRGG LKIAAVKAPG FGDRRKSMLE DIAILTGGTV
ISEELGIKLE NTTMDTLGRA KRIMVDKETT TIVDGAGSKE DIGGRVAQIK AQIEDTTSDY
DREKLQERLA KLAGGVAVIR VGGSTEVEVK EKKDRVDDAL HATRAAVEEG ILPGGGVALL
RVVSALNGLA TANDDQRVGI EIVRRAIEAP VRQIAENAGA EGSIIVGKLR EKQDFAFGWN
AQTGEFGDLF QMGVIDPAKV VRAALQDAAS IAGLLVTTEA MIAEKPKKDG QPQMPPGGGM
DF
