ID A0A1B2R4E0_9BORD Unreviewed; 767 AA.
AC A0A1B2R4E0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Clp protease ClpA {ECO:0000313|EMBL:AOB31824.1};
GN Name=clpA {ECO:0000313|EMBL:AOB31824.1};
GN ORFNames=AKI39_15595 {ECO:0000313|EMBL:AOB31824.1};
OS Bordetella sp. H567.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1697043 {ECO:0000313|EMBL:AOB31824.1, ECO:0000313|Proteomes:UP000093512};
RN [1] {ECO:0000313|Proteomes:UP000093512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H567 {ECO:0000313|Proteomes:UP000093512};
RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A.,
RA Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D.,
RA Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C.,
RA Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V.,
RA Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A.,
RA Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L.,
RA Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H.,
RA Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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; CP012334; AOB31824.1; -; Genomic_DNA.
DR RefSeq; WP_066637862.1; NZ_CP012334.1.
DR AlphaFoldDB; A0A1B2R4E0; -.
DR STRING; 1697043.AKI39_15595; -.
DR KEGG; boh:AKI39_15595; -.
DR PATRIC; fig|1697043.4.peg.3213; -.
DR Proteomes; UP000093512; Chromosome.
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:AOB31824.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AOB31824.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000093512};
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..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 767 AA; 84069 MW; 8F222DEAB5461661 CRC64;
MISQELEVSL HMAFVEARSA RHEFITVEHL LLSLLDNASA VEVLRACAAN LDDLRRNLRQ
FVNENTPVIP SGAEVDTQPT LGFQRVIQRA IMHVSAGGSG KKPVTGANVL VAIFGEKDSH
AVYYLQQQGV TRLDVVNFLS HGITKQPQVE SAASQKEQQP NPEEQGESRQ SPLDQYATDL
NAAALAGRID PLIGRESEVE RVIQVLCRRR KNNPLLVGEA GVGKTAIAEG LAWRITRGEV
PEILQAAQVY ALDMGALLAG TKYRGDFEQR LKGVLKQLRG NPDAILFIDE IHTLIGAGSA
SGGTLDASNL LKPALSSGQL KCIGATTYTE YRGVFEKDHA LSRRFQKIDV SEPSVEQTVQ
ILRGLKTRFE EHHNVRYSAA ALLAAAELSA RHINDRHLPD KAIDVIDEAG AAQRLLPRSR
QKKVIGKVDI ENIVSKIARI PPQSVSNDDR SKLATLDRDL KTVVFGQEAA IEALSASIKM
ARSGLGKPEK PIGAFLFSGP TGVGKTEVAR QLAFTMGVEL LRFDMSEYME RHAVSRLIGA
PPGYVGFDQG GLLTEAITKQ PHCVLLLDEI EKAHPDVFNI LLQVMDHGTL TDNNGRKADF
RNVILIMTTN AGAETLNRPS IGFANARVVG DEMAEIRRMF TPEFRNRLDA IIPFAPLSRE
IILRVVDKFL MQLEDQLHER RVDAVFTETL RAHLAKEGFD PLMGARPMQR LIQDTIRRAL
ADELLFGKLV DGGSVTVDLD QDGKVSLTFG DKPASDAPDA QEVALAE
//
