CH605_SINMW
ID CH605_SINMW Reviewed; 545 AA.
AC A6UM48;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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};
GN OrderedLocusNames=Smed_6084;
OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OG Plasmid pSMED02.
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 pSMED02.";
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; CP000740; ABR64728.1; -; Genomic_DNA.
DR RefSeq; WP_011970828.1; NC_009621.1.
DR RefSeq; YP_001314661.1; NC_009621.1.
DR AlphaFoldDB; A6UM48; -.
DR SMR; A6UM48; -.
DR STRING; 366394.Smed_6084; -.
DR EnsemblBacteria; ABR64728; ABR64728; Smed_6084.
DR KEGG; smd:Smed_6084; -.
DR PATRIC; fig|366394.8.peg.2590; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_5; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 265347at2; -.
DR Proteomes; UP000001108; Plasmid pSMED02.
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..545
FT /note="Chaperonin GroEL 5"
FT /id="PRO_0000332087"
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; 57677 MW; EFF1C8D38CCE95F3 CRC64;
MAAKEVKFGR SAREKMLRGV DILADAVKVT LGPKGRNVVI DKSFGAPRIT KDGVTVAKEI
ELEDKFENMG AQMVREVASK TNDIAGDGTT TATVLAQAIV REGAKAVAAG MNPMDLKRGI
DLAVAEVVKD LLAKAKTINT SDEVAQVGTI SANGEKQIGL DIAEAMQKVG NEGVITVEEA
KTAETELEVV DGMQFDRGYL SPYFVTNPEK MVADLEDAYI 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 KDTDDFGYNA
QTGEYGDMIA MGIIDPVKVV RTALQDAASV ASLLITTEAM IAELPKKDAP AMPGGMGGMG
GMDMM
