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Database: UniProt
Entry: W0VAE8_9BURK
LinkDB: W0VAE8_9BURK
Original site: W0VAE8_9BURK 
ID   W0VAE8_9BURK            Unreviewed;       766 AA.
AC   W0VAE8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:CDG84560.1};
GN   Name=clpA {ECO:0000313|EMBL:CDG84560.1};
GN   ORFNames=GJA_3949 {ECO:0000313|EMBL:CDG84560.1};
OS   Janthinobacterium agaricidamnosum NBRC 102515 = DSM 9628.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=1349767 {ECO:0000313|EMBL:CDG84560.1, ECO:0000313|Proteomes:UP000027604};
RN   [1] {ECO:0000313|EMBL:CDG84560.1, ECO:0000313|Proteomes:UP000027604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102515 / DSM 9628 {ECO:0000313|Proteomes:UP000027604};
RX   PubMed=25883287; DOI=10.1128/genomeA.00277-15;
RA   Graupner K., Lackner G., Hertweck C.;
RT   "Genome Sequence of Mushroom Soft-Rot Pathogen Janthinobacterium
RT   agaricidamnosum.";
RL   Genome Announc. 3:e00277-e00277(2015).
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; HG322949; CDG84560.1; -; Genomic_DNA.
DR   RefSeq; WP_038495030.1; NZ_HG322949.1.
DR   AlphaFoldDB; W0VAE8; -.
DR   STRING; 1349767.GJA_3949; -.
DR   KEGG; jag:GJA_3949; -.
DR   PATRIC; fig|1349767.4.peg.532; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_4; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000027604; Chromosome I.
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:CDG84560.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:CDG84560.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027604};
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          149..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          745..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   766 AA;  84254 MW;  64727BF5F99487EF CRC64;
     MIAQELEVSL HMAFVEARQA RHEFITVEHL LLALLDNPSA AEVLRACAVN LDDLRKTLTN
     FIGDNTPTVP GTGEVDTQPT LGFQRVIQRA IMHVQSASNG KKEVTGANVL VAIFGEKDSH
     AVYYLHQQGV TRLDVVNFIS HGVRKDQQAD SVKASEGVEE APAEGQQKES PLDQFTQNLN
     KAAAEGKIDP LIGREDEVDR VIQILCRRRK NNPLLVGEAG VGKTAIAEGL AWRVTQGDVP
     EILQNAVVYS LDMGALLAGT KYRGDFEQRL KAVLKQLKDN PNGILFIDEI HTIIGAGSAS
     GGTLDASNLL KPALSNGQLK CIGATTYTEF RGVFEKDHAL SRRFQKVDVN EPTVEQTVQI
     LRGLKSRFEE HHGVKYSASA LSTAAELAAR FINDRHLPDK AIDVIDEAGA AQRILPKSKQ
     KKTIGKSEIE DIIAKIARIP PQTVNQDDRS KLQTIDRDLR NVVFGQDPAI EALASAIKMA
     RAGLGKTDKP IGSFLFSGPT GVGKTEVAKQ LAFILGIELI RFDMSEYMER HAVSRLIGAP
     PGYVGFDQGG LLTEAITKKP HAVLLLDEIE KAHPDIFNIL LQVMDHGTLT DNNGRKADFR
     NVIIIMTTNA GAESLQKASI GFTNSKQAGD EMADIKRMFT PEFRNRIDAT ISFRALDEEI
     ILRVVDKFLM QLEEQLHEKK VEAVFTEKLR KFLGKKGFDP LMGARPMSRL IQDMIRKALA
     DELLFGRLVS GGRITVDLDD KDQVKLEFPE SDATPPTSPP ETVEVE
//
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