HTPG_VIBA3
ID HTPG_VIBA3 Reviewed; 634 AA.
AC B7VII6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=VS_2269;
OS Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=575788;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LGP32;
RA Mazel D., Le Roux F.;
RT "Vibrio splendidus str. LGP32 complete genome.";
RL Submitted (FEB-2009) 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; FM954972; CAV19432.1; -; Genomic_DNA.
DR RefSeq; WP_012604546.1; NC_011753.2.
DR AlphaFoldDB; B7VII6; -.
DR SMR; B7VII6; -.
DR STRING; 575788.VS_2269; -.
DR PRIDE; B7VII6; -.
DR EnsemblBacteria; CAV19432; CAV19432; VS_2269.
DR KEGG; vsp:VS_2269; -.
DR PATRIC; fig|575788.5.peg.3531; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_6; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 246194at2; -.
DR Proteomes; UP000009100; 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_1000146010"
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; 71915 MW; 186D203936378FA7 CRC64;
MSETATQNKE TRGFQSEVKQ LLHLMIHSLY SNKEIFLREL ISNASDAADK LRFQALSNGD
LYQGDADLGV KLSFNAEANT LTISDNGIGM SRDNVIEHLG TIAKSGTADF FSKLSEDQSK
DSQLIGQFGV GFYSAFIVAD AVTVRTRAAG LANDQAVQWH SAGEGDYTIE DITKESRGTD
IILHMREDGK EFLNEWRLRE VIGKYSDHIG IPVSIFTAVK DDEGKDTEEK HWEQINKAQA
LWTRNKSDIE KEEYQEFYKH VSHDFADPLT WSHNKVEGKN DYTSLLYIPA KAPWDMMNRD
HKSGLKLYVQ RVFIMDDAEQ FMPSYMRFVR GLIDSNDLPL NVSREILQDN KVTQSLRGAC
TKRVLTMLER MAKNDNDKYL EFWKEFGLVL KEGPAEDMAN KEKIAGLLRF SSTEVDSSEQ
TIGLASYVER MKEGQDKIYY LTADSYAAAK NSPHLEQFKA KGIEVVLMYD RIDEYVMNYL
TDFDGKQFQS ITKAGLDLSK FEGEEEKEKQ KETEEEFKSV VERTQSYLGG RVKEVRTTFK
LATTPAVVVT DDFEMGTQMA KLLEAAGQAA PEVKYIFEIN PEHALVKQMA DEADEQAFGR
WVELLLGQAM LAEKGSMEDP SQFLGAINEL LTKR