CH604_SINMW
ID CH604_SINMW Reviewed; 544 AA.
AC A6UH06;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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};
GN OrderedLocusNames=Smed_4130;
OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OG Plasmid pSMED01.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=366394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA Richardson P.;
RT "Complete sequence of Sinorhizobium medicae WSM419 plasmid pSMED01.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000739; ABR62936.1; -; Genomic_DNA.
DR RefSeq; WP_011969758.1; NC_009620.1.
DR RefSeq; YP_001312869.1; NC_009620.1.
DR AlphaFoldDB; A6UH06; -.
DR SMR; A6UH06; -.
DR PRIDE; A6UH06; -.
DR EnsemblBacteria; ABR62936; ABR62936; Smed_4130.
DR KEGG; smd:Smed_4130; -.
DR PATRIC; fig|366394.8.peg.584; -.
DR HOGENOM; CLU_016503_3_0_5; -.
DR OMA; CVQKIIA; -.
DR OrthoDB; 265347at2; -.
DR Proteomes; UP000001108; Plasmid pSMED01.
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.
FT CHAIN 1..544
FT /note="Chaperonin GroEL 4"
FT /id="PRO_0000332086"
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"
SQ SEQUENCE 544 AA; 57521 MW; 7F8CF5036333558A CRC64;
MSAKEIIFST EVRDRLLRGV ELLNNAVKVT LGPKGRNVVI DRSYGAPRIT KDGVSVAKEI
ELEDKFENMG AQMVREVASK TNDLAGDGTT TATVLAASIF REGAKLVAAG MNPMDLKRGI
DLAVTAVLAE IKLRATKVNS SSEIAQVGTI AANGDASVGE MIAGAMEKVG NEGVITVEEA
RTADTELDVV EGMQFDRGYL SPYFVTNAEK MRVELDDPYI LIHEKKLGNL QTMLPILEAV
VQSGKPLLII SEDVEGEALT TLVVNKLRGG LKIAAVKSPG FGDRRKAMLQ DIAVLTAGQM
ISEDIGIKLE NVTLDMLGRA RRVLIEKDTT TIIDGSGDKA SIQACISQIK AQIEETTSDY
DKEKLQERLA KLTGGVAVIR VGGATELEVK EKKDRIDDAL NATRAAVEEG IVAGGGVALL
RAKSALASLT GENPEITAGI AIVRKALEAP IRQIADNAGV EGSIVIGKLV DSSDQNQGFD
AQTETYVDMI KAGIVDPAKV VRTALRDAGS IAALLITAEA MVADIPEKNA AQNAGNGAMG
GRGY
