ID   HTPG_VIBPA              Reviewed;         634 AA.
AC   Q87RH5;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 1.
DT   25-MAY-2022, entry version 110.
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=VP0821;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000031; BAC59084.1; -; Genomic_DNA.
DR   RefSeq; NP_797200.1; NC_004603.1.
DR   RefSeq; WP_005478520.1; NC_004603.1.
DR   AlphaFoldDB; Q87RH5; -.
DR   SMR; Q87RH5; -.
DR   STRING; 223926.28805807; -.
DR   EnsemblBacteria; BAC59084; BAC59084; BAC59084.
DR   GeneID; 1188318; -.
DR   KEGG; vpa:VP0821; -.
DR   PATRIC; fig|223926.6.peg.778; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000002493; Chromosome 1.
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; Reference proteome;
KW   Stress response.
FT   CHAIN           1..634
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000063021"
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..634
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   634 AA;  72161 MW;  07FA2D276B28B224 CRC64;
     MSETVSQNKE TRGFQSEVKQ LLHLMIHSLY SNKEIFLREL ISNASDASDK LRFQALSNPD
     LYEGNADLGV KLSFDESANT LTISDNGIGM SRNDVIEHLG TIAKSGTAEF FSKLSEEQSK
     DSQLIGQFGV GFYSAFIVAD AVTVRTRAAG LPADEAVQWH SAGEGEYTIE NITKESRGTD
     IILHMRDEGK EFLNEWRLRD VISKYSDHIG IPVSIQTVVR DEDGKETDEK KWEQINKAQA
     LWTRNKADIS DEEYQEFYKH VSHDFADPLV WSHNRVEGKN DYTSLLYIPS KAPWDMMNRD
     HKSGLKLYVQ RVFIMDDAEQ FMPSYLRFVR GLIDSNDLPL NVSREILQDN KVTQSLRNAC
     TKRVLTMLER MAKNDEEKYQ SFWKEFGLVL KEGPAEDFAN KEKIAGLLRF ASTEVDSAEQ
     TVGLASYVER MKEGQDKIYY LTADSYAAAK NSPHLEQFKA KGIEVILMFD RIDEWLMNYL
     TEFDGKQFQS ITKAGLDLSK FEDEADKEKQ KETEEEFKSV VERTKSYLGD RVKDVRTTFK
     LASTPAVVVT DDYEMGTQMA KLLAAAGQAV PEVKYIFEIN PEHELVKRMA DEADEEAFGR
     WVEVLLGQAM LAERGSMEDP TQFLGAINKL LTKV