ID   HTPG_VIBVY              Reviewed;         634 AA.
AC   Q7MMR7;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   25-MAY-2022, entry version 111.
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=VV1000;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC93764.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000037; BAC93764.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_043877094.1; NC_005139.1.
DR   AlphaFoldDB; Q7MMR7; -.
DR   SMR; Q7MMR7; -.
DR   STRING; 672.VV93_v1c09250; -.
DR   EnsemblBacteria; BAC93764; BAC93764; BAC93764.
DR   KEGG; vvy:VV1000; -.
DR   PATRIC; fig|196600.6.peg.998; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000002675; 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; Reference proteome;
KW   Stress response.
FT   CHAIN           1..634
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000063023"
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;  72339 MW;  08AF3667B6C93452 CRC64;
     MNETVANNKE TRGFQSEVKQ LLHLMIHSLY SNKEIFLREL ISNASDAADK LRFQALSNPA
     LYENDAELGV KLSFNEEHNT LTISDNGIGM SREEVISHLG TIAKSGTAEF FSKLSQEQSK
     DSQLIGQFGV GFYSAFIVAD AVTVRTRAAG LNADQAVLWH SAGEGEYTVE DITKESRGTD
     IILHMREDGK EFLNEWRLRD VIGKYSDHIG IPVSIQTRVR DEEGKETEEV KWEQINKAQA
     LWTRNKSDIS DEEYQEFYKH VSHDFADPLL WSHNRVEGKN DYTSLLYIPS KAPWDMMNRD
     HKSGLKLYVQ RVFIMDDAEQ FMPSYLRFVR GLIDSNDLPL NVSREILQDN KVTQSLRGAC
     TKRVLTMLER LAKNDTEKYQ TFWKEFGLVM KEGPAEDYAN REKVAALLRF ASTEVDSAEQ
     TVSLESYVER MKEGQDKIYY LTADSYAAAK NSPHLEQFKA KGLEVILMFD RIDEWLMNYL
     TEFDGKQFQS ITKAGLDLSQ FEDEQEKEKQ KETEQEFQSV VERTKSYLGD RVKEVRTTFK
     LANTPAVVVT DDFEMGTQMA KLLAAAGQAV PEVKYIFEIN PNHTLVKQMA DEADEEAFGR
     WVEVLLGQAM LAERGSMEDP SQFLTAINSL LTKG