HTPG_VIBVU
ID HTPG_VIBVU Reviewed; 634 AA.
AC Q8DFM0;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=VV1_0189;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) 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; AE016795; AAO08726.1; -; Genomic_DNA.
DR RefSeq; WP_011078304.1; NC_004459.3.
DR AlphaFoldDB; Q8DFM0; -.
DR SMR; Q8DFM0; -.
DR PRIDE; Q8DFM0; -.
DR EnsemblBacteria; AAO08726; AAO08726; VV1_0189.
DR KEGG; vvu:VV1_0189; -.
DR HOGENOM; CLU_006684_3_0_6; -.
DR OMA; MRRMKEM; -.
DR Proteomes; UP000002275; 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..634
FT /note="Chaperone protein HtpG"
FT /id="PRO_0000063022"
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; 72344 MW; 97BDAAB7EB330EFE CRC64;
MNETVANNKE TRGFQSEVKQ LLHLMIHSLY SNKEIFLREL ISNASDAADK LRFQALSNPA
LYENDAELGV KLSFNEEHNT LTISDNGIGM SREEVISHLG TIAKSGTAEF FSKLSQEQSK
DSQLIGQFGV GFYSAFIVAD AVTVRTRAAG LSADQAVLWH SAGEGEYTVE DITKESRGTD
IILHMREDGK EFLNEWRLRD VIGKYSDHIG IPVSIQTRVR DEEGKETEEV KWEQINKAQA
LWTRNKSDIS DEEYQEFYKH VSHDFADPLL WSHNRVEGKN DYTSLLYIPS KAPWDMMNRD
HKSGLKLYVQ RVFIMDDAEQ FMPSYLRFVR GLIDSNDLPL NVSREILQDN KVTQSLRGAC
TKRVLTMLER LAKNDTDKYQ TFWKEFGLVM KEGPAEDYAN REKVASLLRF ASTEVDSAEQ
TVSLESYVER MKEGQDKIYY LTADSYAAAK NSPHLEQFKA KGLEVILMFD RIDEWLMNYL
TEFDGKQFQS ITKAGLDLSQ FEDEQEKEKQ KETEQEFQSV VERTKSYLGD RVKEVRTTFK
LANTPAVVVT DDFEMGTQMA KLLAAAGQAV PEVKYIFEIN PNHTLVKQMA DETDEEAFGR
WVEVLLGQAM LAERGSMEDP SQFLTAINSL LTKG
