ID Q3BW16_XANC5 Unreviewed; 656 AA.
AC Q3BW16;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=Putative Hsp90-family heat shock protein {ECO:0000313|EMBL:CAJ22947.1};
GN OrderedLocusNames=XCV1316 {ECO:0000313|EMBL:CAJ22947.1};
OS Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=316273 {ECO:0000313|Proteomes:UP000007069};
RN [1] {ECO:0000313|EMBL:CAJ22947.1, ECO:0000313|Proteomes:UP000007069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=85-10 {ECO:0000313|EMBL:CAJ22947.1,
RC ECO:0000313|Proteomes:UP000007069};
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., Schneicker 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 -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM039952; CAJ22947.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3BW16; -.
DR STRING; 456327.BJD11_16100; -.
DR KEGG; xcv:XCV1316; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_028672_0_0_6; -.
DR Proteomes; UP000007069; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF26; HEAT SHOCK PROTEIN (HSP90 FAMILY)-RELATED; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Stress response {ECO:0000313|EMBL:CAJ22947.1}.
FT REGION 21..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 72811 MW; 33BA5CBED31E0477 CRC64;
MRAMWVPASL SGWHWHPGGR VRGWASSPRK RRPIMQDPTP EATDASQIRR AGVDLNGLMS
VLGKHLYSTP VVALRELVQN AHDSILRRRL EQPDWDGQSR IEVHADTAQG IVRIVDTGAG
LTQQEIHDYL ATVGVGYTRG LRQGGHEDSG LIGMFGLGFL SAFVLARRVT VRTTSYQSPT
LGYCYISSNA EQYTVSPIPA RAQVGTEVVL ELHGDYLSLA QEGRLREILS RYCALLREPI
WIGAATQPIN PEPPPWRVQD AVPLHPVQAW RRQREFAARF ERNFEPLCCM PVRAEEGSDA
VGLLWVQDGA TYGTSDNRNL SVFLRGMLLD DNARELLPPW AGFIGGVIES NRLTPTASRE
DLQRDTVYSA VQHALSEALV QGLADVARQQ PEAWRRILLR HNEALLGAAL CDERLFELLL
EHVRVPTSQG DLPAQQLPSR GAVHVILDSD SGFEEMLFRA MGVPVAYGNR YAVVPFLRRW
AQVKGVRLVE LGTEQGNRQL FQLDTLPADE LAWLEQHLGD GEALVPARFS PQELPLVVVP
DREAELKRRL EQDENDKRVS TAALRLARQF TARIQARQTQ RLYLNLDNPA LQALLGAQRA
GNPQAAVAAR LLRALKVIVA AQGRTQPQPG STESGVSDLN KAFGDFAETV TQLLAR
//
