HTPG_XANC5
ID HTPG_XANC5 Reviewed; 634 AA.
AC Q3BS21;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=XCV2711;
OS Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=316273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=85-10;
RX PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA Kaiser O.;
RT "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT genome sequence.";
RL J. Bacteriol. 187:7254-7266(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; AM039952; CAJ24388.1; -; Genomic_DNA.
DR RefSeq; WP_011347837.1; NZ_CP017190.1.
DR AlphaFoldDB; Q3BS21; -.
DR SMR; Q3BS21; -.
DR STRING; 456327.BJD11_09300; -.
DR PRIDE; Q3BS21; -.
DR EnsemblBacteria; CAJ24388; CAJ24388; XCV2711.
DR KEGG; xcv:XCV2711; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_6; -.
DR OMA; MRRMKEM; -.
DR Proteomes; UP000007069; Chromosome.
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_0000224238"
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; 70868 MW; CF98920B7CC5CBBA CRC64;
MTVETDKQTL GFQTEVKQLL QLMIHSLYSN KEIFLRELVS NAADAADKLR FEALVKPELL
EGSGELRIRV DYDKDARTVT IDDNGIGMSR EEAVSHLGTI AKSGTADFLK HLSGDQKKDA
NLIGQFGVGF YSAFIVADQV DVYSRRAGLP ASEGVHWSSR GEGEFEIASV DKPERGTRIV
LHLKEGEESF ADGWTLRGIL KKYSDHIGLP IEMRKEHYGE AADKPAEPEW EAVNRASALW
TRPKSEIKDE EYQEFYKHIA HDAGNPLAWS HNKVEGKLEY TSLLFVPGRA PFDLYHRDSA
KGLKLYVQRV FIMDQAEQFL PLYLRFIKGV VDSSDLSLNV SREILQSGPV VDSMKSALTK
RSLDMLEKLA KDKPDDYATF WRNFGQALKE GPAEDYANRE KIAGLLRFSS THDTTGAQSV
GLADYVSRLA EGQDKLYYLT GESYAQIKDS PHLEVFRKKG IEVLLLTDRI DEWLMSYLTE
FDGKSFVDVA RGDLDLGKLD SEEDKKAQED LAKSKEGLAS RIKAALGDDV AEVRVSHRLT
DSPAILAIGQ GDLGLQMRQL LEASGQAVPE SKPVFEFNPT HPLIEKLDAE QDMDRFGDLS
RVLFDQAALA AGDSLKDPAA YVRRLNKLLL ELSV