ID   HTPG_ALISL              Reviewed;         632 AA.
AC   B6EHJ9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=VSAL_I0814;
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238;
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(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; FM178379; CAQ78499.1; -; Genomic_DNA.
DR   RefSeq; WP_012549603.1; NC_011312.1.
DR   AlphaFoldDB; B6EHJ9; -.
DR   SMR; B6EHJ9; -.
DR   STRING; 316275.VSAL_I0814; -.
DR   PRIDE; B6EHJ9; -.
DR   EnsemblBacteria; CAQ78499; CAQ78499; VSAL_I0814.
DR   KEGG; vsa:VSAL_I0814; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001730; 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; Stress response.
FT   CHAIN           1..632
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000146004"
FT   REGION          1..343
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          344..560
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          561..632
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   632 AA;  71668 MW;  30DA2F137DE50505 CRC64;
     MSEQTINNKE TRGFQSEVKQ LLHLMIHSLY SNKEIFLREL ISNASDASDK LRFKALSNGD
     LYEGNADLGV KISFNVEANT LTISDNGIGM GREDVIEHLG TIAKSGTADF FSKLSEDQSK
     DSQLIGQFGV GFYSAFIVAD AVTVRTRVAG AAKDQAVQWH SEGEGDYTIE DVTKESRGTD
     IILHMRDEGK EFLSEWRLKE VIGKYSDHIG IPVSIWTVEK DEEGKETEGK WEQVNKAQAL
     WTRNKSEIED AEYQEFYKHV SHDFADPLTW SHNKVEGKND YTSLLYIPAK APFDMMNRDH
     KSGLKLYVQR VFVMDDAEQF MPSYLRFVKG LIDSNDLALN VSREILQDNK VTQSLRGACT
     KRVLSMLEKI AKKDNDKYLS FWKEFGQVLK EGLAEDFANK DKIAGLLRFA STNKDSSEQA
     ISLASYVERM KEDQDKIFYL TSDSYAAAKN SPHLEQFKSK GIEVVLMYDR IDEWLMSYLT
     EFDGKQFQSI TKAGLDLSKF ENEAEKEKQK ETTEEFKSVV ERTKAYLGDR VKEVRTTFKL
     ATTPAVVVTD DFEMGTQMAK LLEAAGQAAP EVKYIFEINP EHALIKQMAD EADEEAFGRW
     VEMLLGQAML AERGSLDDPS QFLSAMNQLL SK