CH602_MYCBO
ID CH602_MYCBO Reviewed; 540 AA.
AC P0A521; A0A1R3XXI1; P06806; Q48920; Q48931; X2BF25;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Chaperonin GroEL 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=65 kDa antigen;
DE AltName: Full=Antigen A;
DE AltName: Full=Cell wall protein A;
DE AltName: Full=Chaperonin-60 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Heat shock protein 65;
GN Name=groEL2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL2 {ECO:0000255|HAMAP-Rule:MF_00600}, hsp65;
GN OrderedLocusNames=BQ2027_MB0448;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BCG;
RX PubMed=3553003; DOI=10.1128/iai.55.6.1466-1475.1987;
RA Thole J.E.R., Keulen W.J., Kolk A.H.J., Groothuis D.G., Berwald L.G.,
RA Tiesjema R.H., van Embden J.D.A.;
RT "Characterization, sequence determination, and immunogenicity of a 64-
RT kilodalton protein of Mycobacterium bovis BCG expressed in Escherichia coli
RT K-12.";
RL Infect. Immun. 55:1466-1475(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-196.
RC STRAIN=356;
RA Ros C., Belak K.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-183.
RC STRAIN=ATCC 19210 / NCTC 10772 / TMC 410, and TMC 1024;
RX PubMed=7848059;
RA Kapur V., Li L.L., Hamrick M.R., Plikaytis B.B., Shinnick T.M., Telenti A.,
RA Jacobs W.R. Jr., Banerjee A., Cole S., Yuen K.Y., Clarridge J.E.,
RA Kreiswirth B.N., Musser J.M.;
RT "Rapid Mycobacterium species assignment and unambiguous identification of
RT mutations associated with antimicrobial resistance in Mycobacterium
RT tuberculosis by automated DNA sequencing.";
RL Arch. Pathol. Lab. Med. 119:131-138(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 65-178.
RX PubMed=2507865; DOI=10.1111/j.1365-2958.1989.tb00233.x;
RA Hance A.J., Grandchamp B., Levy-Frebault V., Lecossier D., Rauzier J.,
RA Bocart D., Gicquel B.;
RT "Detection and identification of mycobacteria by amplification of
RT mycobacterial DNA.";
RL Mol. Microbiol. 3:843-849(1989).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RC STRAIN=BCG / Pasteur;
RX PubMed=16006064; DOI=10.1016/j.femsle.2005.06.004;
RA Dosanjh N.S., Rawat M., Chung J.-H., Av-Gay Y.;
RT "Thiol specific oxidative stress response in Mycobacteria.";
RL FEMS Microbiol. Lett. 249:87-94(2005).
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: Secreted, capsule {ECO:0000250|UniProtKB:P9WPE7}.
CC Cell surface {ECO:0000250|UniProtKB:P9WPE7}. Secreted, cell wall
CC {ECO:0000250|UniProtKB:P9WPE7}.
CC -!- INDUCTION: Induced in response to the thiol oxidant diamide.
CC {ECO:0000269|PubMed:16006064}.
CC -!- MISCELLANEOUS: Purified 65 kDa antigen can elicit a strong delayed-type
CC hypersensitivity reaction in experimental animals infected with
CC M.tuberculosis. This protein is one of the major immunoreactive
CC proteins of the mycobacteria. This antigen contains epitopes that are
CC common to various species of mycobacteria.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; M17705; AAA25358.1; -; Genomic_DNA.
DR EMBL; LT708304; SIT99035.1; -; Genomic_DNA.
DR EMBL; U55833; AAC44451.1; -; Genomic_DNA.
DR EMBL; U17925; AAB39044.1; -; Genomic_DNA.
DR PIR; A43509; A43509.
DR PIR; S05292; S05292.
DR RefSeq; NP_854111.1; NC_002945.3.
DR RefSeq; WP_003402236.1; NC_002945.4.
DR AlphaFoldDB; P0A521; -.
DR SMR; P0A521; -.
DR GeneID; 45424401; -.
DR PATRIC; fig|233413.5.peg.488; -.
DR OMA; TDTDKME; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0042603; C:capsule; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; 2.
DR SUPFAM; SSF52029; SSF52029; 1.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell wall; Chaperone; Isomerase; Nucleotide-binding; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..540
FT /note="Chaperonin GroEL 2"
FT /id="PRO_0000063424"
FT REGION 521..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 86..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ SEQUENCE 540 AA; 56727 MW; FF034616F709DA2A CRC64;
MAKTIAYDEE ARRGLERGLN ALADAVKVTL GPKGRNVVLE KKWGAPTITN DGVSIAKEIE
LEDPYEKIGA ELVKEVAKKT DDVAGDGTTT ATVLAQALVR EGLRNVAAGA NPLGLKRGIE
KAVEKVTETL LKGAKEVETK EQIAATAAIS AGDQSIGDLI AEAMDKVGNE GVITVEESNT
FGLQLELTEG MRFDKGYISG YFVTDPERQE AVLEDPYILL VSSKVSTVKD LLPLLEKVIG
AGKPLLIIAE DVEGEALSTL VVNKIRGTFK SVAVKAPGFG DRRKAMLQDM AILTGGQVIS
EEVGLTLENA DLSLLGKARK VVVTKDETTI VEGAGDTDAI AGRVAQIRQE IENSDSDYDR
EKLQERLAKL AGGVAVIKAG AATEVELKER KHRIEDAVRN AKAAVEEGIV AGGGVTLLQA
APTLDELKLE GDEATGANIV KVALEAPLKQ IAFNSGLEPG VVAEKVRNLP AGHGLNAQTG
VYEDLLAAGV ADPVKVTRSA LQNAASIAGL FLTTEAVVAD KPEKEKASVP GGGDMGGMDF
