CH605_RHIME
ID CH605_RHIME Reviewed; 542 AA.
AC P35471;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Chaperonin GroEL 5 {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin 5 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 5 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 5 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL5 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL5 {ECO:0000255|HAMAP-Rule:MF_00600}; OrderedLocusNames=RB1006;
GN ORFNames=SMb21566;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2).
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=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(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}.
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DR EMBL; M94191; AAA26287.1; -; Genomic_DNA.
DR EMBL; AL591985; CAC49406.1; -; Genomic_DNA.
DR PIR; F95967; F95967.
DR PIR; JN0512; JN0512.
DR RefSeq; NP_437546.1; NC_003078.1.
DR RefSeq; WP_010975850.1; NC_003078.1.
DR AlphaFoldDB; P35471; -.
DR SMR; P35471; -.
DR STRING; 266834.SM_b21566; -.
DR EnsemblBacteria; CAC49406; CAC49406; SM_b21566.
DR GeneID; 61600966; -.
DR KEGG; sme:SM_b21566; -.
DR PATRIC; fig|266834.11.peg.5931; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_5; -.
DR OMA; LKDQHMN; -.
DR Proteomes; UP000001976; Plasmid pSymB.
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; Plasmid;
KW Reference proteome; Stress response.
FT CHAIN 1..542
FT /note="Chaperonin GroEL 5"
FT /id="PRO_0000063504"
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 239
FT /note="A -> R (in Ref. 1; AAA26287)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="L -> V (in Ref. 1; AAA26287)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="A -> G (in Ref. 1; AAA26287)"
FT /evidence="ECO:0000305"
FT CONFLICT 534..538
FT /note="LPAGG -> FRPR (in Ref. 1; AAA26287)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 57882 MW; 200FAC54B6736245 CRC64;
MAAKEVKFQT DARERMLRGV DVLANAVKVT LGPKGRNVVI DKSFGAPRIT KDGVSVAKEI
ELEDKFENMG AQMLREVASR TNDLAGDGTT TATVLAQAIV REGAKAVASG MNPMDLKRGI
DLAVDAVVKE LKNNARKISK NSEIAQVGTI SANGDTEIGR YLAEAMEKVG NEGVITVEEA
KTAETELEVV EGMQFDRGYL SPYFITNQDK MRVELEDPYI LIHEKKLSNL QAMLPVLEAV
VQSGKPLLII AEDVEGEALA TLVVNKLRGG LKVAAVKAPG FGDRRKAMLE DIAILTGGTV
VSEDLGIKLE SVTLDMLGRA KKVSIEKENT TIIDGAGSKA DIEGRTAQIR AQIEETTSDY
DREKLQERLA KLAGGVAVIR VGGSTEVEVK EKKDRVDDAL HATRAAVEEG ILPGGGVALL
RAVKALDGLK TANNDQRVGV DLVRRAIEAP VRQIAENAGA EGSIIVGKLR EKTEFSYGWN
AQTNEYGDLY AMGVIDPAKV VRTALQDAAS VAGLLVTTEA MIAEKPKKEA APALPAGGGM
DF
