ID   HTPG_VIBCH              Reviewed;         635 AA.
AC   P22359; Q9KTB8;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 138.
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=VC_0985;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-110.
RC   STRAIN=ATCC 55056 / El Tor Ogawa E7946;
RX   PubMed=2124707; DOI=10.1073/pnas.87.24.9898;
RA   Parsot C., Mekalanos J.J.;
RT   "Expression of ToxR, the transcriptional activator of the virulence factors
RT   in Vibrio cholerae, is modulated by the heat shock response.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:9898-9902(1990).
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   -!- INDUCTION: By increase in temperature.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00505}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA27574.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE003852; AAF94146.1; -; Genomic_DNA.
DR   EMBL; M58033; AAA27574.1; ALT_INIT; Genomic_DNA.
DR   PIR; A39266; A39266.
DR   PIR; B82255; B82255.
DR   RefSeq; NP_230631.1; NC_002505.1.
DR   RefSeq; WP_001889892.1; NZ_LT906614.1.
DR   AlphaFoldDB; P22359; -.
DR   SMR; P22359; -.
DR   STRING; 243277.VC_0985; -.
DR   DNASU; 2614238; -.
DR   EnsemblBacteria; AAF94146; AAF94146; VC_0985.
DR   GeneID; 57739672; -.
DR   KEGG; vch:VC_0985; -.
DR   PATRIC; fig|243277.26.peg.938; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   BioCyc; VCHO:VC0985-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0009408; P:response to heat; IBA:GO_Central.
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; IPR019805; Heat_shock_protein_90_CS.
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; PF02518; HATPase_c; 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.
DR   PROSITE; PS00298; HSP90; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..635
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000063019"
FT   REGION          1..344
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          345..561
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          562..635
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   635 AA;  72197 MW;  A635C6A38C151AAC CRC64;
     MSETATTNKE TRGFQSEVKQ LLHLMIHSLY SNKEIFLREL ISNASDAVDK LRFQALSHPD
     LYQGDAELGV KLSFDKDKNT LTISDNGIGM TRDEVIENLG TIAKSGTAEF FSKLSQEQSK
     NSQLIGQFGV GFYSAFIVAD AVTVRTRAAG SAPADAVQWY SKGEGEYTVE TINKESRGTD
     IILHLREEGK EFLSEWRLRD VISKYSDHIG IPVYIQTSVM DEEGKATEET KWEQINKAQA
     LWTRAKSEVT DEEYKEFYKH VSHDFADPLV WSHNKVEGKN DYTSLLYIPA KAPWDLFNRE
     HKHGLKLYVQ RVFIMDDAAQ FMPSYLRFVR GLIDSNDLPL NVSREILQDN KITQSLRQAC
     TKRVLTMLER MASNDADNYQ KFWKEFGLVM KEGPAEDFAN REKIASLLRF ASTHIDSAEQ
     TISLASYVER MKEGQDKIYY LTADSYTAAK NSPHLEQFKS KGIEVILMFD RIDEWLMNYL
     PEFEGKAFQS ITKAGLDLSQ FEDEAEKEKH KETEEQFKSV VERLKGYLGS RVKEVRTTFK
     LANTPAVVVT DDYEMGTQMA KLLAAAGQPV PEVKYILEVN PEHALVKRMA DEADEQTFGR
     WAEVLLGQAM LAERGSMEDP SQFLGAVNQL LAPSH