ID   HTPG_VIBC1              Reviewed;         634 AA.
AC   A7N178;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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};
GN   OrderedLocusNames=VIBHAR_01327;
OS   Vibrio campbellii (strain ATCC BAA-1116).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2902295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA   Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA   Wilson R.K.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000789; ABU70304.1; -; Genomic_DNA.
DR   RefSeq; WP_012127249.1; NC_022269.1.
DR   AlphaFoldDB; A7N178; -.
DR   SMR; A7N178; -.
DR   PRIDE; A7N178; -.
DR   EnsemblBacteria; ABU70304; ABU70304; VIBHAR_01327.
DR   KEGG; vha:VIBHAR_01327; -.
DR   PATRIC; fig|338187.25.peg.1321; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000008152; 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..634
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014964"
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;  71948 MW;  7266E935034DF409 CRC64;
     MSETVSHNKE TRGFQSEVKQ LLHLMIHSLY SNKEIFLREL ISNASDASDK LRFQALSNPD
     LYEGNADLGV KLAFDESANT LTISDNGIGM SRDDVIEHLG TIAKSGTAEF FSKLSDDQSK
     DSQLIGQFGV GFYSAFIVAD AVTVCTRAAG LAADEAVQWQ SAGEGDYTVE TITKDSRGTD
     IVLHMREEGK EFLNEWRLRD VISKYSDHIG IPVSIQTSVR DDEGKETGEK KWEQINKAQA
     LWTRNKSEIS EEEYQEFYKH VSHDFADPLT WSHNRVEGKN DYTSLLYIPA KAPWDMMNRD
     HKSGLKLYVQ RVFIMDDAEQ FMPSYMRFVR GLIDSNDLPL NVSREILQDN KVTQSLRNAC
     TKRVLTMLDR MAKNDTEKYQ SFWKEFGLVM KEGVAEDMAN KEKVAGLLRF ASTEVDSAEQ
     TVGLASYVER MKEGQDKIYF LTADSYAAAK NSPHLEQFRA KGIEVILMFD RIDEWLMNYL
     TEFDGKQFQS ITKAGLDLSK FEDEAEKEKQ KETEEEFKSV VERTQSYLGD RVKEVRTTFK
     LATTPAVVVT DDFEMGTQMA KLLEAAGQAV PEVKYIFEIN PEHALVKRMA DEADEEVFGR
     WVEVLLGQAM LAERGSMEDP SQFVGAINKL LTKV