ID S5TUE5_ENTCL Unreviewed; 546 AA. AC S5TUE5; A0A0P8I575; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 22-FEB-2023, entry version 71. DE RecName: Full=Chaperonin GroEL {ECO:0000256|HAMAP-Rule:MF_00600}; DE EC=5.6.1.7 {ECO:0000256|HAMAP-Rule:MF_00600}; DE AltName: Full=60 kDa chaperonin {ECO:0000256|HAMAP-Rule:MF_00600}; DE AltName: Full=Chaperonin-60 {ECO:0000256|HAMAP-Rule:MF_00600}; DE Short=Cpn60 {ECO:0000256|HAMAP-Rule:MF_00600}; GN Name=groEL {ECO:0000256|HAMAP-Rule:MF_00600, GN ECO:0000313|EMBL:AGS56781.1}; GN Synonyms=groL {ECO:0000256|HAMAP-Rule:MF_00600, GN ECO:0000313|EMBL:AHN60531.1}; GN ORFNames=pCRE727_16 {ECO:0000313|EMBL:AHN60531.1}, pNDM1_EC14653_00120 GN {ECO:0000313|EMBL:AKN19823.1}, pYQ13500_017 GN {ECO:0000313|EMBL:AKP49212.1}; OS Enterobacter cloacae. OG Plasmid pCR16-ECL-NDM-1 {ECO:0000313|EMBL:AKN35257.1}, OG Plasmid pECL3-NDM-1 {ECO:0000313|EMBL:AGS56781.1}, OG Plasmid pNDM-ECN49 {ECO:0000313|EMBL:AKJ21421.1}, OG Plasmid pNDM-Ec1GN574 {ECO:0000313|EMBL:AIM48565.1}, OG Plasmid pNDM-HF727 {ECO:0000313|EMBL:AHN60531.1}, OG Plasmid pNDM1_EC14653 {ECO:0000313|EMBL:AKN19823.1}, OG Plasmid pPN2-ECL-NDM-1 {ECO:0000313|EMBL:ALD19765.1}, and OG Plasmid pYQ13500-NDM {ECO:0000313|EMBL:AKP49212.1}. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=550 {ECO:0000313|EMBL:AGS56781.1}; RN [1] {ECO:0000313|EMBL:AHN60531.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CRE727 {ECO:0000313|EMBL:AHN60531.1}; RC PLASMID=pNDM-HF727 {ECO:0000313|EMBL:AHN60531.1}; RA Ho P.L., Li Z., Lo W.U., Cheung Y.Y., Lin C.H., Sham P.C., Cheng V.C.C., RA Ng T.K., Que T.L., Chow K.H.; RT "Identification and characterization of a novel incompatibility group X3 RT plasmid carrying blaNDM-1 in Enterobacteriaceae isolates with RT epidemiological links to multiple geographical areas in China."; RL Emerg. Microbes Infect. 1:e39-e39(2012). RN [2] {ECO:0000313|EMBL:AHN60531.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CRE727 {ECO:0000313|EMBL:AHN60531.1}; RC PLASMID=pNDM-HF727 {ECO:0000313|EMBL:AHN60531.1}; RA Ho P.L., Lo W.U., Li Z., Chow K.H., Lin C.H., Chan W.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AIM48565.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GN574 {ECO:0000313|EMBL:AIM48565.1}; RC PLASMID=pNDM-Ec1GN574 {ECO:0000313|EMBL:AIM48565.1}; RX PubMed=25845877; DOI=10.1128/AAC.04862-14; RA Tijet N., Richardson D., MacMullin G., Patel S.N., Melano R.G.; RT "Characterization of multiple NDM-1-producing Enterobacteriaceae isolates RT from the same patient."; RL Antimicrob. Agents Chemother. 59:3648-3651(2015). RN [4] {ECO:0000313|EMBL:AKN19823.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WCHECl-14653 {ECO:0000313|EMBL:AKN19823.1}; RC PLASMID=pNDM1_EC14653 {ECO:0000313|EMBL:AKN19823.1}; RX PubMed=26248381; DOI=10.1128/AAC.01275-15; RA Wu W., Feng Y., Carattoli A., Zong Z.; RT "Characterization of an Enterobacter cloacae Strain Producing both KPC and RT NDM Carbapenemases by Whole-Genome Sequencing."; RL Antimicrob. Agents Chemother. 59:6625-6628(2015). RN [5] {ECO:0000313|EMBL:AKP49212.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=EC-YQ13500 {ECO:0000313|EMBL:AKP49212.1}; RC PLASMID=pYQ13500-NDM {ECO:0000313|EMBL:AKP49212.1}; RX PubMed=26047502; RA Yang Q., Fang L., Fu Y., Du X., Shen Y., Yu Y.; RT "Dissemination of NDM-1-Producing Enterobacteriaceae Mediated by the IncX3- RT Type Plasmid."; RL PLoS ONE 10:E0129454-E0129454(2015). RN [6] {ECO:0000313|EMBL:AKN35257.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CR16 {ECO:0000313|EMBL:AKN35257.1}; RC PLASMID=pCR16-ECL-NDM-1 {ECO:0000313|EMBL:AKN35257.1}; RA Wailan A.M., Paterson D.L., Kennedy K., Ingram P., Paterson D.L., RA Sidjabat H.E.; RT "Genomic characteristics of NDM-producing Enterobacteriaceae in Australia RT and their blaNDM genetic contexts."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:ALD19765.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Pn2 {ECO:0000313|EMBL:ALD19765.1}; RC PLASMID=pPN2-ECL-NDM-1 {ECO:0000313|EMBL:ALD19765.1}; RA Wailan A.M., Sartor A.L., Zowawi H.M., Perry J.D., Paterson D.L., RA Sidjabat H.E.; RT "The genetic characterization of NDM-1 producing Enterobacteriaceae and RT Acinetobacter baumannii from Pakistan hospitals for an insight of blaNDM RT acquisition via plasmids."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:AKJ21421.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ECN49 {ECO:0000313|EMBL:AKJ21421.1}; RC PLASMID=pNDM-ECN49 {ECO:0000313|EMBL:AKJ21421.1}; RA Zhao X.J., Ma P.; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000313|EMBL:AGS56781.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ECL3 {ECO:0000313|EMBL:AGS56781.1}; RC PLASMID=pECL3-NDM-1 {ECO:0000313|EMBL:AGS56781.1}; RX PubMed=27114281; RA Wailan A.M., Sidjabat H.E., Yam W.K., Alikhan N.F., Petty N.K., RA Sartor A.L., Williamson D.A., Forde B.M., Schembri M.A., Beatson S.A., RA Paterson D.L., Walsh T.R., Partridge S.R.; RT "Mechanisms involved in acquisition of blaNDM genes by IncA/C2 and IncFIIY RT plasmids."; RL Antimicrob. Agents Chemother. 0:0-0(2016). 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:0000256|HAMAP-Rule:MF_00600, CC ECO:0000256|RuleBase:RU000419}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an CC unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00600, ECO:0000256|RuleBase:RU000419}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00600}. CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. CC {ECO:0000256|ARBA:ARBA00006607, ECO:0000256|HAMAP-Rule:MF_00600, CC ECO:0000256|RuleBase:RU000418}. 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; KC887917; AGS56781.1; -; Genomic_DNA. DR EMBL; KF976405; AHN60531.1; -; Genomic_DNA. DR EMBL; KJ812998; AIM48565.1; -; Genomic_DNA. DR EMBL; KP765744; AKJ21421.1; -; Genomic_DNA. DR EMBL; KP868647; AKN19823.1; -; Genomic_DNA. DR EMBL; KP826704; AKN35257.1; -; Genomic_DNA. DR EMBL; KR059865; AKP49212.1; -; Genomic_DNA. DR EMBL; KP770024; ALD19765.1; -; Genomic_DNA. DR RefSeq; WP_004201176.1; NZ_RXQP01000050.1. DR RefSeq; YP_009023656.1; NC_023914.1. DR AlphaFoldDB; S5TUE5; -. DR SMR; S5TUE5; -. DR GeneID; 69461758; -. 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; 3.50.7.10; GroEL; 1. DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1. DR Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 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 PANTHER; PTHR45633; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1. DR PANTHER; PTHR45633:SF3; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR SUPFAM; SSF52029; GroEL apical domain-like; 1. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1. DR TIGRFAMs; TIGR02348; GroEL; 1. DR PROSITE; PS00296; CHAPERONINS_CPN60; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00600}; KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00600}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00600}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00600}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00600}; Plasmid {ECO:0000313|EMBL:AGS56781.1}; KW Stress response {ECO:0000313|EMBL:AGS56781.1}. FT REGION 527..546 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 30..33 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00600" FT BINDING 51 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00600" FT BINDING 87..91 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00600" FT BINDING 415 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00600" FT BINDING 479..481 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00600" FT BINDING 495 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00600" SQ SEQUENCE 546 AA; 57062 MW; 4E48091CE2FC367A CRC64; MAAKDIRFGE DARSKMVRGV NVLANAVKAT LGPKGRNVVL QKSYGAPTIT KDGVSVAKEI ELADAFENMG AQMVKEVASK TSDNAGDGTT TATVLAQAFI REGMKAVAAG MNPMDLKRGI DQAVKAAVGE LKSLSKPSST SKEIAQVGAI SANSDANIGD LIAQAMDKVG KEGVITVEEG SGLDNELDVV EGMQFDRGYL SPYFVNNQQS MSADLDDPFI LLYDKKISNV RDLLPVLEGV AKAGKPLLIV AEEVEGEALA TLVVNTIRGI VKVCAVKAPG FGDRRKAMLE DMAILTGGVV ISEEVGLSLE KATIKDLGRA KKIQVSKENT TIIDGAGEGA GIEARIKQIK AQIEETSSDY DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG IVPGGGVALI RAKAAIAGIK GVNEDQNHGI QIALRAMEAP LREIVTNAGD EPSVILNRVV EGSGAFGYNA ANGEFGDMIE FGILDPTKVT RTALQNAASI AGLMITTEAM VAEAPKKDEP AMPAGGGMGG MGGMDF //