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Database: UniProt
Entry: Q63WJ0_BURPS
LinkDB: Q63WJ0_BURPS
Original site: Q63WJ0_BURPS 
ID   Q63WJ0_BURPS            Unreviewed;       766 AA.
AC   Q63WJ0;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   24-JAN-2024, entry version 117.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:CAH34893.1};
GN   Name=clpA {ECO:0000313|EMBL:CAH34893.1};
GN   Synonyms=lopD {ECO:0000313|EMBL:CAH34893.1};
GN   OrderedLocusNames=BPSL0899 {ECO:0000313|EMBL:CAH34893.1};
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH34893.1, ECO:0000313|Proteomes:UP000000605};
RN   [1] {ECO:0000313|EMBL:CAH34893.1, ECO:0000313|Proteomes:UP000000605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243 {ECO:0000313|EMBL:CAH34893.1,
RC   ECO:0000313|Proteomes:UP000000605};
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA   Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA   Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA   Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA   Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA   Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA   Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA   Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA   Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; BX571965; CAH34893.1; -; Genomic_DNA.
DR   RefSeq; WP_004196461.1; NZ_CP009538.1.
DR   RefSeq; YP_107526.1; NC_006350.1.
DR   AlphaFoldDB; Q63WJ0; -.
DR   STRING; 272560.BPSL0899; -.
DR   GeneID; 56594754; -.
DR   KEGG; bps:BPSL0899; -.
DR   PATRIC; fig|272560.51.peg.683; -.
DR   eggNOG; COG0542; Bacteria.
DR   OMA; GRVIQEH; -.
DR   Proteomes; UP000000605; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043335; P:protein unfolding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR013461; ClpA.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR02639; ClpA; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF111; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 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.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Hydrolase {ECO:0000313|EMBL:CAH34893.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:CAH34893.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000605};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          147..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   766 AA;  84115 MW;  116698E3CC09894C CRC64;
     MIAQELEVSL HMAFMEARQA RHEFITVEHL LLALLDNPTA AEVLRACAAN IEDLRQNLRN
     FIHDNTPTVP GTDDVDTQPT LGFQRVIQRA IMHVQSTSNG KKEVTGANVL VAIFGEKDSH
     AVYYLQQQGV TRLDVVNFIS HGIAKTSSGE AAKPADANAE GEDAGAQKET PLAQFTQNLN
     QMAKDGRIDP LIGRESEVER VVQVLCRRRK NNPLLVGEAG VGKTAIAEGL AYRITRGEVP
     DILANAQVYS LDMGALLAGT KYRGDFEQRL KTVLKELKER PHAILFIDEI HTLIGAGAAS
     GGTLDASNLL KPALSSGTLK CIGATTFTEY RGIFEKDAAL SRRFQKIDVT EPSVEQTVAI
     LRGLKSRFEE HHGVKYSSGA LSAAAELSAR FITDRHLPDK AIDVIDEAGA AQRVLPKSKQ
     KKTIGKSEIE EIISKIARVP PQSVSQDDRS KLQTLDRDLK SVVFGQDPAI DALAAAIKMA
     RAGLGKLDKP IGAFLFSGPT GVGKTEVARQ LAFTLGIELI RFDMSEYMER HAVSRLIGAP
     PGYVGFDQGG LLTEAVTKKP HCVLLLDEIE KAHPDIFNVL LQVMDHGTLT DNNGRKADFR
     NVIIIMTTNA GAESMQKATI GFTTRRETGD EMADIKRLFT PEFRNRLDAT ISFRSLDEEI
     IMRVVDKFLI QLEEQLHEKK VDALFTDALR KHLAKHGFDP LMGARPMQRL IQDTIRRALA
     DELLFGKLVN GGHVTVDVDE NDKVLLSFDK TATPPSKPNE EAVEVE
//
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