CH60_NEIGO
ID CH60_NEIGO Reviewed; 544 AA.
AC P29842;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 116.
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;
GN Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600}, hsp63, mopA;
OS Neisseria gonorrhoeae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PID 2, and VP1 / 830563;
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 PROTEIN SEQUENCE OF 1-27, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=VP1 / 830563;
RX PubMed=1400243; DOI=10.1128/jb.174.21.6928-6937.1992;
RA Pannekoek Y., van Putten J.P.M., Dankert J.;
RT "Identification and molecular analysis of a 63-kilodalton stress protein
RT from Neisseria gonorrhoeae.";
RL J. Bacteriol. 174:6928-6937(1992).
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: Cell outer membrane {ECO:0000269|PubMed:1400243};
CC Peripheral membrane protein {ECO:0000269|PubMed:1400243}.
CC -!- INDUCTION: By iron limitation, glucose deprivation, and growth under
CC low oxygen supply. {ECO:0000269|PubMed:1400243}.
CC -!- MISCELLANEOUS: This protein shows ATPase activity.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; Z23008; CAA80550.1; -; Genomic_DNA.
DR EMBL; Z23009; CAA80551.1; -; Genomic_DNA.
DR PIR; S61300; S61300.
DR PIR; S61301; S61301.
DR AlphaFoldDB; P29842; -.
DR SMR; P29842; -.
DR PRIDE; P29842; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
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 1: Evidence at protein level;
KW ATP-binding; Cell outer membrane; Chaperone; Direct protein sequencing;
KW Isomerase; Membrane; Nucleotide-binding.
FT CHAIN 1..544
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063457"
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 VARIANT 106
FT /note="A -> Y (in strain: PID 2)"
FT VARIANT 298
FT /note="A -> G (in strain: PID 2)"
FT VARIANT 437
FT /note="D -> E (in strain: PID 2)"
FT VARIANT 451
FT /note="L -> V (in strain: PID 2)"
FT VARIANT 494
FT /note="L -> H (in strain: PID 2)"
FT VARIANT 541..543
FT /note="Missing (in strain: PID 2)"
FT CONFLICT 13
FT /note="R -> C (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 57241 MW; 2D902B3D591D7655 CRC64;
MAAKDVQFGN EVRQKMVNGV NILANAVRVT LGPKGRNVVV DRAFGGPHIT KDGVTVAKEI
ELKDKFENMG AQMVKEVASK TNDVAGDGTT TATVLAQSIV AEGIKAVTAG MNPTDLKRGI
DKAVAALVEE LKNIAKPCDT SKEIAQVGSI SANSDEQVGA IIAEAMEKVG KEGVITVEDG
KSLENELDVV EGMQFDRGYL SPYFINDAEK QIAGLDNPFV LLFDKKISNI RDLLPVLEQV
AKASRPLLII AEDVEGEALA TLVVNNIRGV LKTVAVKAPG FGDRRKAMLQ DIAILTGAVV
ISEEVGLSLE KATLDDLGQA KRIEIGKENT TVIDGFGDAA QIEARVAEIR QQIETATSDY
DKEKLQERVA KLAGGVAVIK VGAATEVEMK EKKDRVEDAL HATRAAVEEG VVAGGGVALL
RARAALENLH TGNADQDAGV QIVLRAVESP LRQIVANAGG EPSVVVNKVL EGKGNYGYNA
GSGEYGDMIG MGVLDPAKVT RSALQHAASI AGLMLTTDCM IAEIPEEKPA VPDMGGMGGM
GGMM
