ID   HTPG_VIBCM              Reviewed;         635 AA.
AC   C3LTN3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=VCM66_0941;
OS   Vibrio cholerae serotype O1 (strain M66-2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=579112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M66-2;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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; CP001233; ACP05259.1; -; Genomic_DNA.
DR   RefSeq; WP_001889892.1; NC_012578.1.
DR   AlphaFoldDB; C3LTN3; -.
DR   SMR; C3LTN3; -.
DR   EnsemblBacteria; ACP05259; ACP05259; VCM66_0941.
DR   GeneID; 57739672; -.
DR   KEGG; vcm:VCM66_0941; -.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000001217; Chromosome I.
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; 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   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT   CHAIN           1..635
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000146009"
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