ID   HTPG_MYCPA              Reviewed;         644 AA.
AC   P61186;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Chaperone protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE   AltName: Full=Heat shock protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE   AltName: Full=High temperature protein G {ECO:0000255|HAMAP-Rule:MF_00505};
GN   Name=htpG {ECO:0000255|HAMAP-Rule:MF_00505}; OrderedLocusNames=MAP_2069c;
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 [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: Molecular chaperone. Has ATPase activity. {ECO:0000255|HAMAP-
CC       Rule:MF_00505}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00505}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00505}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00505}.
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DR   EMBL; AE016958; AAS04386.1; -; Genomic_DNA.
DR   RefSeq; WP_010949465.1; NC_002944.2.
DR   AlphaFoldDB; P61186; -.
DR   SMR; P61186; -.
DR   STRING; 262316.MAP_2069c; -.
DR   EnsemblBacteria; AAS04386; AAS04386; MAP_2069c.
DR   KEGG; mpa:MAP_2069c; -.
DR   PATRIC; fig|262316.17.peg.2193; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_11; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000000580; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.790; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..644
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000062995"
FT   REGION          1..352
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          353..566
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          567..644
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   644 AA;  72828 MW;  8C9D1CFD2FD7F560 CRC64;
     MNARVEQLEF QAEARQLLDL MVHSVYSNKD SFLRELISNA SDALDKLRLE AFRNKDLDVD
     TSDLHIQIEV DKDARTLTIR DNGIGMTRAE VVDLIGTLAK SGTAELRQQL REAKNAQNEA
     ASEELIGQFG IGFYSSFMVA DKVELLTRKA GESEATKWES SGEGTYTIES VENAPQGTSV
     TLHLKPEDTE DELHDYTSEF KIKSLVKKYS DFIAWPIRME VERRTPATEE GGEETVTREV
     ETLNSMKALW ARPKDEVSEE EYKEFYKHIA HAWDDPLEVI AMKAEGTFEY QALLFIPSHA
     PFDLFNRDAH TGIQLYVKRV FIMGDCDQLM PEYLRFVKGV VDAQDMSLNV SREILQQDRQ
     IKAIRRRLTK KVLSTIKELQ SERLDDYRTF WTQFGRVVKE GLLSDFDNQE TLVQLCSFAS
     THSEEEATTL AQYVERMKEG QTQIFYATGE TRQQILKSPH LEAFKAKGYE VLLLTDPVDE
     VWVGTVTEFD GKPLQSIAKG EVDLSAEGEE SQAERDEQQK EFADLLAWLK DTLSDHVKEV
     RLSNRLTDSP ACLITDAFGI TPALARLYRA SGQDIPVGKR ILELNPKHPL VTGLRQAHQD
     RADDPSVAET AELLYGTALL AEGGALDDPA RFAEILADRL ARTL