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Database: UniProt
Entry: F9S5C0_9VIBR
LinkDB: F9S5C0_9VIBR
Original site: F9S5C0_9VIBR 
ID   F9S5C0_9VIBR            Unreviewed;       634 AA.
AC   F9S5C0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Chaperone protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE   AltName: Full=Heat shock protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE   AltName: Full=High temperature protein G {ECO:0000256|HAMAP-Rule:MF_00505};
GN   Name=htpG {ECO:0000256|HAMAP-Rule:MF_00505};
GN   ORFNames=VII00023_18999 {ECO:0000313|EMBL:EGU35931.1};
OS   Vibrio ichthyoenteri ATCC 700023.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=870968 {ECO:0000313|EMBL:EGU35931.1, ECO:0000313|Proteomes:UP000004605};
RN   [1] {ECO:0000313|EMBL:EGU35931.1, ECO:0000313|Proteomes:UP000004605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700023 {ECO:0000313|EMBL:EGU35931.1,
RC   ECO:0000313|Proteomes:UP000004605};
RX   PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA   Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA   McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT   "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT   Scleritoderma cyanea.";
RL   Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
CC   -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000256|HAMAP-
CC       Rule:MF_00505}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00505}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239, ECO:0000256|HAMAP-Rule:MF_00505}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00505}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGU35931.1}.
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DR   EMBL; AFWF01000217; EGU35931.1; -; Genomic_DNA.
DR   RefSeq; WP_006713700.1; NZ_AFWF01000217.1.
DR   AlphaFoldDB; F9S5C0; -.
DR   OrthoDB; 9802640at2; -.
DR   Proteomes; UP000004605; Unassembled WGS sequence.
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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   CDD; cd16927; HATPase_Hsp90-like; 1.
DR   Gene3D; 3.30.230.80; -; 1.
DR   Gene3D; 3.40.50.11260; -; 1.
DR   Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00505};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00505};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00505};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW   ECO:0000313|EMBL:EGU35931.1}.
FT   DOMAIN          32..189
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          1..344
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT   REGION          562..634
FT                   /note="C"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   634 AA;  72354 MW;  6614F7128F79733F CRC64;
     MSETATHNKE TRGFQSEVKQ LLHLMIHSLY SNKEIFLREL ISNASDASDK LRFQALSNAD
     LYQGDADLSV KLSFDQKNNT LTISDNGIGM SREDVIEHLG TIAKSGTAEF FSKLSDDQSK
     DSQLIGQFGV GFYSAFIVAD SVTVRTRAAN LSADQAVQWH SEGEGDYTIE DIHKETRGTD
     IVLHMREDGK EFLNEWRLRD VIGKYSDHIG IPVLIHTEER DEEGKETGEK KWEQINKAQA
     LWTRNKSDIS DEEYQEFYKH VSHDFADPLV WSHNRVEGKN DYTSLLYIPA KAPWDMFNRD
     HKSGLKLYVQ RVFIMDDAEQ FMPSYLRFIR GLIDSNDLPL NVSREILQDN KVTQSLRNAC
     TKRVLTMLER MANNDNDKYL SFWKEFGLVL KEGPAEDMSN KEKVAGLLRF ASTEVDSEEQ
     TVGLASYVER MKEDQDKIYY LTADSYAAAK NSPHLEQFKA KGIEVILMYD RIDEWLMNYL
     TEFDGKQFQS ITKAGLDLSK FEDEAEKEKH KAAEEEFKSV VERTKEYLGD RVKEVRTTFK
     LATTPAVVVT DDFEMGTQMA KLLEAAGQAV PEVKYIFEIN PEHPLVKQMA DEADEQAFGR
     WVEVLLGQAM LAERGSLQDP SQFLGAINSL LTKG
//
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