ID A0A0H4W5U2_9BORD Unreviewed; 769 AA.
AC A0A0H4W5U2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:AKQ56136.1};
GN Name=clpA {ECO:0000313|EMBL:AKQ56136.1};
GN ORFNames=ACR54_02823 {ECO:0000313|EMBL:AKQ56136.1}, CS347_16785
GN {ECO:0000313|EMBL:AZW18301.1};
OS Bordetella hinzii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=103855 {ECO:0000313|EMBL:AKQ56136.1, ECO:0000313|Proteomes:UP000036382};
RN [1] {ECO:0000313|EMBL:AKQ56136.1, ECO:0000313|Proteomes:UP000036382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F582 {ECO:0000313|EMBL:AKQ56136.1,
RC ECO:0000313|Proteomes:UP000036382};
RX PubMed=26316634;
RA Weigand M.R., Changayil S., Kulasekarapandian Y., Tondella M.L.;
RT "Complete Genome Sequences of Two Bordetella hinzii Strains Isolated from
RT Humans.";
RL Genome Announc. 3:e00965-e00915(2015).
RN [2] {ECO:0000313|Proteomes:UP000036382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F582 {ECO:0000313|Proteomes:UP000036382};
RA Weigand M.R., Changayil S., Kulasekarapandian Y., Batra D., Williams M.M.,
RA Tondella M.L.;
RT "Complete Genome Sequences of Two Bordetella hinzii Isolated from Humans.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000282741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H720 {ECO:0000313|Proteomes:UP000282741};
RA Weigand M.R., Loparev V., Peng Y., Bowden K.E., Tondella M.L.,
RA Williams M.M.;
RT "Whole genome sequencing of various Bordetella species.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AZW18301.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H720 {ECO:0000313|EMBL:AZW18301.1};
RX PubMed=31744907;
RA Weigand M.R., Peng Y., Batra D., Burroughs M., Davis J.K., Knipe K.,
RA Loparev V.N., Johnson T., Juieng P., Rowe L.A., Sheth M., Tang K.,
RA Unoarumhi Y., Williams M.M., Tondella M.L.;
RT "Conserved Patterns of Symmetric Inversion in the Genome Evolution of
RT Bordetella Respiratory Pathogens.";
RL mSystems 4:e00702-19(2019).
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; CP012076; AKQ56136.1; -; Genomic_DNA.
DR EMBL; CP024172; AZW18301.1; -; Genomic_DNA.
DR RefSeq; WP_029579592.1; NZ_LT906461.1.
DR STRING; 103855.ACR54_02823; -.
DR GeneID; 56621816; -.
DR KEGG; bhz:ACR54_02823; -.
DR PATRIC; fig|103855.14.peg.2788; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000036382; Chromosome.
DR Proteomes; UP000282741; 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:AKQ56136.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AKQ56136.1};
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 144..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 769 AA; 84507 MW; 6C70F8C32B6A135B CRC64;
MISQELEVSL HMAFVEARSA RHEFITVEHL LLSLLDNASA VEVLRACAAN LDDLRRNLRQ
FVTENTPVIP SGAEVDTQPT LGFQRVIQRA IMHVSAGGTG KKPVTGANVL VAIFGEKDSH
AVYYLQQQGV TRLDVVNFLS HGITKQPQEE PSAVQKEQQS PGEEGGESRQ SPLDQYANDL
NAAALAGRID PLIGREHEVE RVIQVLCRRR KNNPLLVGEA GVGKTAIAEG LAWRITRGEV
PEILQSAQVY ALDMGALLAG TKYRGDFEQR LKGVLKQIRG NPDAVLFIDE IHTLIGAGSA
SGGTLDASNL LKPALSSGQL KCIGATTYTE YRGVFEKDHA LSRRFQKIDV PEPSVDQTVQ
ILRGLKSRFE EHHSVRYSAA ALSAAAELSA RYINDRHLPD KAIDVIDEAG AAQRLLPRSR
QKKVIGKAEI EAIVSKIARI PPQSVSSDDR SKLATLDRDL KTVVFGQDQA IDALAAAIKM
ARSGLGKPDK PIGAFLFSGP TGVGKTEVAR QLAFTLGVEL LRFDMSEYME RHAVSRLIGA
PPGYVGFDQG GLLTEAIAKQ PHCVLLLDEI EKAHPDIFNI LLQVMDHGTL TDNNGRKADF
RNVILIMTTN AGAETLNRAA IGFTNTRVVG DEMAEIRRMF TPEFRNRLDA IIPFAPLDRE
IILRVVDKFL MQLEDQLHER RVEAVFTEKL RDYLAKHGFD PLMGARPMQR LIQDTIRRAL
ADELLFGRLV DGGNVTVDLD ENDKVVLSFD EAAKSTPSAK DKPEVELVD
//