HTPG_XANOM
ID HTPG_XANOM Reviewed; 634 AA.
AC Q2P2U8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=XOO2374;
OS Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=342109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 311018;
RA Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT large numbers of effector genes and insertion sequences to its race
RT diversity.";
RL Jpn. Agric. Res. Q. 39:275-287(2005).
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; AP008229; BAE69129.1; -; Genomic_DNA.
DR RefSeq; WP_011408651.1; NC_007705.1.
DR AlphaFoldDB; Q2P2U8; -.
DR SMR; Q2P2U8; -.
DR KEGG; xom:XOO2374; -.
DR HOGENOM; CLU_006684_3_0_6; -.
DR OMA; MRRMKEM; -.
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_0000237006"
FT REGION 1..342
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 343..559
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 560..634
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 634 AA; 70889 MW; D4EBA1C17AFCF3E8 CRC64;
MTVDTDKQTL GFQTEVKQLL QLMIHSLYSN KEIFLRELVS NAADAADKLR FEALVKPELL
EGSGELRIRV DYDKDARTVT IDDNGIGMSR EDAVSHLGTI AKSGTADFLK HLSGDQKKDA
NLIGQFGVGF YSAFIVADQV DVYSRRAGLP AREGVHWSSR GEGEFEVASV DKPERGTRIV
LHLKDGEDTF ADGWTLRGIL KKYSDHIGLP IEMRKEHYGE AADKPAEPEW EAVNRASALW
TRPKSEIKDE EYQEFYKHIA HDAGNPLAWS HNKVEGKLEY TSLLFVPGRA PFDLYHRDSA
KGLKLYVQRV FIMDQAEQFL PLYLRFIKGV VDSSDLSLNV SREILQSGPV VDSMKSALTK
RSLDMLEKLA KDKPDDYATF WRNFGQALKE GPAEDYANRE KIAGLMRFSS THDTTGAQSV
GLADYVSRLA EGQDKLYYLT GESYAQIKDS PHLEVFRKKG IEVLLLTDRI DEWLMSYLTE
FDGKSFVDVA RGDLDLGKLD SEEDKKAQEE VAKSKEGLAS RIKAALGEDV AEVRVSHRLT
DSPAILAIGQ GDLGLQMRQL LEASGQAVPE SKPVFEFNPT HPLIEKLDAE QDMDRFCDLS
QVLFDQAALA AGDSLKDPAG YVKRLNKLLL ELSV
