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Database: UniProt
Entry: A9WSY2_RENSM
LinkDB: A9WSY2_RENSM
Original site: A9WSY2_RENSM 
ID   A9WSY2_RENSM            Unreviewed;       623 AA.
AC   A9WSY2;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Chaperone protein {ECO:0000313|EMBL:ABY23920.1};
GN   Name=htpG {ECO:0000313|EMBL:ABY23920.1};
GN   OrderedLocusNames=RSal33209_2188 {ECO:0000313|EMBL:ABY23920.1};
OS   Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS   NBRC 15589 / NCIMB 2235).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Renibacterium.
OX   NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY23920.1, ECO:0000313|Proteomes:UP000002007};
RN   [1] {ECO:0000313|Proteomes:UP000002007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC   {ECO:0000313|Proteomes:UP000002007};
RX   PubMed=18723615; DOI=10.1128/JB.00721-08;
RA   Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA   Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA   Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT   "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT   reductive evolution away from an environmental Arthrobacter ancestor.";
RL   J. Bacteriol. 190:6970-6982(2008).
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; CP000910; ABY23920.1; -; Genomic_DNA.
DR   RefSeq; WP_012245586.1; NC_010168.1.
DR   AlphaFoldDB; A9WSY2; -.
DR   STRING; 288705.RSal33209_2188; -.
DR   KEGG; rsa:RSal33209_2188; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_028672_0_0_11; -.
DR   Proteomes; UP000002007; 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   Reference proteome {ECO:0000313|Proteomes:UP000002007}.
SQ   SEQUENCE   623 AA;  68231 MW;  523EA637DAD0ED0A CRC64;
     MTQESTERPF QVDLRGVVDL LSRHIYSTPQ VYLRELMQNG VDAISARKLQ DPNAEPGRIR
     IEHNGARLTV SDNGVGLTLD EAAQLLATVG RSSKRDSVLN LRREDFLGQF GIGLLSCFLV
     TDNIRVRSRS ATGSQAIEWV GSAEGTFTLR SLDEDDIPVG TTIVLDPRPD DAALLSRETV
     QRLALHYGQY LPVSIDVNGQ AINRTPPFLN ADLLDTAFLG KGTASGSELQ ELRELGKELL
     GAQPLDAIRI DIPGTGTRGV AFVLPSAPPP SAHQANRAYL GRMLLSDRVD DLLPDWAFFV
     RCVVDTTGLQ PTASREQLVE DSALEFTREE LGKILKRWIV QLATTQPSRF DQFLAVHQLA
     LRSLALYDDE LAQVIVPWLS VETASGRVSC RELIEAGGSI RYTETVDEFR QIAAVVPAGT
     VVVNGGYTYE SEFIRGLVRL NPALSVERIR VAEVLDELSA PSLEHREVTA GLEQRAEAAL
     AESHCKVSVR LFAPEQLPAL YVADPEVLRR IEREKSAELA PGFWAGIMNK VDAQLNATAG
     DSGEAPTSRL CLNWATPLMR ELATVRDEVV FDRTVRLLYV QAMLEGHRPL TTADRAMLTG
     SLTDLIHLSV TADFGTTAGP EAL
//
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