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Database: UniProt
Entry: Q13YG7_PARXL
LinkDB: Q13YG7_PARXL
Original site: Q13YG7_PARXL 
ID   Q13YG7_PARXL            Unreviewed;       916 AA.
AC   Q13YG7;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   24-JAN-2024, entry version 112.
DE   SubName: Full=ClpA/B-type chaperone, ATPase subunit ClpB, heat shock protein {ECO:0000313|EMBL:ABE30872.1};
GN   ORFNames=Bxe_A2096 {ECO:0000313|EMBL:ABE30872.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE30872.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE30872.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE30872.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC       involved in the recovery of the cell from heat-induced damage, in
CC       cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the
CC       processing of protein aggregates. Protein binding stimulates the ATPase
CC       activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC       which probably helps expose new hydrophobic binding sites on the
CC       surface of ClpB-bound aggregates, contributing to the solubilization
CC       and refolding of denatured protein aggregates by DnaK.
CC       {ECO:0000256|ARBA:ARBA00025613}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675}.
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DR   EMBL; CP000270; ABE30872.1; -; Genomic_DNA.
DR   RefSeq; WP_011488485.1; NZ_CP008760.1.
DR   AlphaFoldDB; Q13YG7; -.
DR   STRING; 266265.Bxe_A2096; -.
DR   KEGG; bxb:DR64_4251; -.
DR   KEGG; bxe:Bxe_A2096; -.
DR   PATRIC; fig|266265.5.peg.2443; -.
DR   eggNOG; COG0542; Bacteria.
DR   OMA; HRDVHEM; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR017729; ATPase_T6SS_ClpV1.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR03345; VI_ClpV1; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF184; ATPASE WITH CHAPERONE ACTIVITY-RELATED; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 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   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:ABE30872.1}.
FT   DOMAIN          9..151
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
SQ   SEQUENCE   916 AA;  98166 MW;  ADB81848CF4E8A08 CRC64;
     MAISRQALFG KLGTTLYRSI ESATAFCKLR GNPYIELVHW LHQLLQQPDS DLHRLVRHCG
     IERETLDRDM ARALAALPAG ASSISDFSHH VELAVERAWV LATLSFNDRR IRSAWLVAAL
     VQTPELRRVL LSISPAFGKL SVVGLDEALP AYMENSPEAA EAPYDNSNFS TAVPGEASHA
     LPAQSKGSPL EQFCTDLTVR AHSGEIDPVV GRELEIRTMI DVLLRRRQNN PLLTGEAGVG
     KTAVVEGLAC AIATGNVPPR LVGVRLLSLD VGALLAGASM KGEFELRLRG VLEAALKSAV
     PVILFVDEIH TLIGAGGQAG TGDAANLLKP ALARGAIRMI GATTWAEYKR HIEKDAALTR
     RFQVLQVRQP QEPAAIDMVR GLANTFSRHH GVVVRDQAIR AAVRLSHRYI PSRQLPDKAI
     SLLDTACARV ALSQHAPPRE LQDARQRVLA ARVESELLVA ESRIGLDTAS ALAAARTRIG
     ELVAVEERIE ARWKAQLAAA QALLAARDAA LGADHGAPHT GANSDACASP DSLKDLERAL
     TQLQGDAPLV FPEVSEAIVA EVVSDWTGIP VGRMVTDEVA AVQSLPATLE ARVIGQPDAL
     RQIGERVQTA RAGLTDPKKP LGVFLLAGPS GVGKTETALA LAEALYGGEQ NLITVNMSEY
     QEAHTVSGLK GAPPGYVGYG EGGVLTEAVR RRPYSVVLLD EIEKAHRDVH EMFFQVFDKG
     YMEDGDGRYI DFRNTTILLT SNAGSELIAS LCADAPLPPD AEGLREALTP ALLNAFPAAF
     LGRVTVVPYR PLAHESLARI VRLHLDRVVT RMAQVHDIAL AYSGQVVDYI VGRCLVQETG
     ARVLIGFIEQ HVLPRLSALW LDALASKQPI TRIEIGVVDA SAPPTAALAF PCTYAHAPAM
     PAAAATPSTL SVAQVD
//
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