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
//