CH602_MYCPA
ID CH602_MYCPA Reviewed; 541 AA.
AC P42384;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 141.
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=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, mopA;
GN OrderedLocusNames=MAP_3936;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=18;
RA Bujdoso R.;
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43015 / CIP 103965 / Linda;
RX PubMed=8574825; DOI=10.1128/cdli.2.6.657-664.1995;
RA El-Zaatari F.A.K., Naser S.A., Engstrand L., Burch P.E., Hachem C.Y.,
RA Whipple D.L., Graham D.Y.;
RT "Nucleotide sequence analysis and seroreactivities of the 65K heat shock
RT protein from Mycobacterium paratuberculosis.";
RL Clin. Diagn. Lab. Immunol. 2:657-664(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(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 -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA99670.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X74518; CAA52630.1; -; Genomic_DNA.
DR EMBL; U15989; AAA99670.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE016958; AAS06486.1; -; Genomic_DNA.
DR PIR; A37335; A37335.
DR PIR; S40245; S40245.
DR RefSeq; WP_010950172.1; NC_002944.2.
DR AlphaFoldDB; P42384; -.
DR SMR; P42384; -.
DR STRING; 262316.MAP_3936; -.
DR PRIDE; P42384; -.
DR EnsemblBacteria; AAS06486; AAS06486; MAP_3936.
DR KEGG; mpa:MAP_3936; -.
DR PATRIC; fig|262316.17.peg.4188; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_11; -.
DR OMA; TDTDKME; -.
DR Proteomes; UP000000580; 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; 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; Cell wall; Chaperone; Isomerase; Nucleotide-binding;
KW Reference proteome; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..541
FT /note="Chaperonin GroEL 2"
FT /id="PRO_0000063442"
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 476..478
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"
FT VARIANT 45
FT /note="A -> S (in strain: Linda)"
FT VARIANT 481
FT /note="E -> K (in strain: Linda)"
FT VARIANT 491..492
FT /note="AD -> TE (in strain: Linda)"
FT VARIANT 508
FT /note="A -> S (in strain: Linda)"
FT VARIANT 525
FT /note="A -> T (in strain: Linda)"
FT VARIANT 527
FT /note="A -> P (in strain: Linda)"
FT CONFLICT 429
FT /note="L -> P (in Ref. 1; CAA52630)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="A -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 56643 MW; 1D3F40031FF2F780 CRC64;
MAKTIAYDEE ARRGLERGLN ALADAVKVTL GPKGRNVVLE KKWGAPTITN DGVSIAKEIE
LEDPYEKIGA ELVKEVAKKT DDVAGDGTTT ATVLAQALVR EGLRNVAAGA NPLGLKRGIE
KAVEKVTETL LKSAKEVETK DQIAATAAIS AGDQSIGDLI AEAMDKVGNE GVITVEESNT
FGLQLELTEG MRFDKGYISG YFVTDAERQE AVLEDPFILL VSSKVSTVKD LLPLLEKVIQ
AGKPLLIIAE DVEGEALSTL VVNKIRGTFK SVAVKAPGFG DRRKAMLQDM AILTGGQVIS
EEVGLSLESA DISLLGKARK VVVTKDETTI VEGAGDSDAI AGRVAQIRTE IENSDSDYDR
EKLQERLAKL AGGVAVIKAG AATEVELKER KHRIEDAVRN AKAAVEEGIV AGGGVALLHA
IPALDELKLE GEEATGANIV RVALEAPLKQ IAFNGGLEPG VVAEKVRNSP AGTGLNAATG
EYEDLLKAGI ADPVKVTRSA LQNAASIAGL FLTTEAVVAD KPEKAAAPAG DPTGGMGGMD
F
