CH60_NEIMB
ID CH60_NEIMB Reviewed; 544 AA.
AC P42385;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Chaperonin GroEL {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=63 kDa stress protein;
DE AltName: Full=Chaperonin-60 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=GSP63;
DE AltName: Full=HSP60;
GN Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600}, hsp63, mopA;
GN OrderedLocusNames=NMB1972;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CCUG 23106 / 2996 / Serogroup B / Serotype 2b;
RX PubMed=7746149; DOI=10.1111/j.1365-2958.1995.tb02242.x;
RA Pannekoek Y., Dankert J., van Putten J.P.M.;
RT "Construction of recombinant neisserial Hsp60 proteins and mapping of
RT antigenic domains.";
RL Mol. Microbiol. 15:277-285(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=NZ98/254 / Serogroup B;
RX PubMed=16645985; DOI=10.1002/pmic.200500821;
RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.;
RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine
RT prepared from the group B strain NZ98/254.";
RL Proteomics 6:3400-3413(2006).
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 -!- MISCELLANEOUS: Present in outer membrane vesicle formulations which are
CC used as vaccines in human.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; Z22956; CAA80532.1; -; Genomic_DNA.
DR EMBL; AE002098; AAF42301.1; -; Genomic_DNA.
DR PIR; C81021; C81021.
DR PIR; S61303; S61303.
DR RefSeq; NP_274966.1; NC_003112.2.
DR RefSeq; WP_002214867.1; NC_003112.2.
DR AlphaFoldDB; P42385; -.
DR SMR; P42385; -.
DR STRING; 122586.NMB1972; -.
DR PaxDb; P42385; -.
DR EnsemblBacteria; AAF42301; AAF42301; NMB1972.
DR KEGG; nme:NMB1972; -.
DR PATRIC; fig|122586.8.peg.2514; -.
DR HOGENOM; CLU_016503_3_0_4; -.
DR OMA; TDTDKME; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:1990220; C:GroEL-GroES complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..544
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063460"
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"
FT CONFLICT 129
FT /note="D -> E (in Ref. 1; CAA80532)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="A -> G (in Ref. 1; CAA80532)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="D -> E (in Ref. 1; CAA80532)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="Q -> K (in Ref. 1; CAA80532)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="D -> N (in Ref. 1; CAA80532)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="V -> T (in Ref. 1; CAA80532)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="S -> F (in Ref. 1; CAA80532)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="D -> N (in Ref. 1; CAA80532)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="V -> F (in Ref. 1; CAA80532)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="V -> L (in Ref. 1; CAA80532)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="Q -> K (in Ref. 1; CAA80532)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="P -> S (in Ref. 1; CAA80532)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="D -> N (in Ref. 1; CAA80532)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="V -> M (in Ref. 1; CAA80532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 57423 MW; BC619AAB9B5701C1 CRC64;
MAAKDVQFGN EVRQKMVNGV NILANAVRVT LGPKGRNVVV DRAFGGPHIT KDGVTVAKEI
ELKDKFENMG AQMVKEVASK TNDVAGDGTT TATVLAQSIV AEGMKYVTAG MNPTDLKRGI
DKAVAALVDE LKNIAKPCDT SKEIAQVGSI SANSDEQVGA IIAEAMEKVG KEGVITVEDG
KSLENELDVV EGMQFDRGYL SPYFINDAEK QIAALDNPFV LLFDKKISNI RDLLPVLEQV
AKASRPLLII AEDVEGEALA TLVVNNIRGI LKTVAVKAPG FGDRRKAMLQ DIAILTGGVV
ISEEVGLSLE KATLDDLGQA KRIEIGKENT TIIDGFGDAA QIEARVAEIR QQIETATSDY
DKEKLQERVA KLAGGVAVIK VGAATEVEMK EKKDRVEDAL HATRAAVEEG VVAGGGVALL
RARAALENLH TGNADQDAGV QIVLRAVESP LRQIVANAGG EPSVVVNKVL EGKGNYGYNA
GSGEYGDMIE MGVLDPAKVT RSALQHAASI AGLMLTTDCM IAEIPEDKPA VPDMGGMGGM
GGMM
