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Entry: A0A0H4W5U2_9BORD
LinkDB: A0A0H4W5U2_9BORD
Original site: A0A0H4W5U2_9BORD 
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
//
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