ID J2U978_9BURK Unreviewed; 768 AA.
AC J2U978;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit clpA {ECO:0000313|EMBL:EJL87782.1};
GN ORFNames=PMI16_02668 {ECO:0000313|EMBL:EJL87782.1};
OS Herbaspirillum sp. CF444.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1144319 {ECO:0000313|EMBL:EJL87782.1, ECO:0000313|Proteomes:UP000007296};
RN [1] {ECO:0000313|EMBL:EJL87782.1, ECO:0000313|Proteomes:UP000007296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF444 {ECO:0000313|EMBL:EJL87782.1,
RC ECO:0000313|Proteomes:UP000007296};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJL87782.1}.
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DR EMBL; AKJW01000061; EJL87782.1; -; Genomic_DNA.
DR RefSeq; WP_007880229.1; NZ_AKJW01000061.1.
DR AlphaFoldDB; J2U978; -.
DR STRING; 1144319.PMI16_02668; -.
DR PATRIC; fig|1144319.3.peg.2704; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000007296; Unassembled WGS sequence.
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:EJL87782.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:EJL87782.1};
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 146..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 768 AA; 84863 MW; C5DDBB069DF7E130 CRC64;
MIAQELEVSL HMAFVEARQS RHEFITVEHL LLALLDNPSA AEVLRACSVN IDDLRKTLTN
FITDNTPTVP GTNEVDTQPT LGFQRVIQRA IMHVQSASNG KKEVTGANVL VAIFGEKDSH
AVYYLHQQGV TRLDVVNFIS HGVRKDQQVD SQKAPEGAED VQTEGQQKES PLDQFTQNLN
KAAAEGKIDP LIGRDAEVER VIQTLCRRRK NNPLLVGEAG VGKTAIAEGL AWRITQSDVP
EILKNAVVYS LDMGALLAGT KYRGDFEQRL KAVLKQLKDS PNGILFIDEI HTIIGAGSAS
GGTLDASNLL KPALSSGQLK CIGATTYTEF RGVFEKDHAL SRRFQKIDVN EPTVEQTIQI
LRGLKSKFEE HHGVKYSASA LTSAAELAAR FINDRHLPDK AIDVIDEAGA AQRILPKSKQ
KKTIGKSEIE EIISKIARIP PQSVNQDDRT KLQTIDRDLK NVVFGQDPAI EALASAIKMA
RAGLGKTDKP IGSFLFSGPT GVGKTEVAKQ LAFILGIELI RFDMSEYMER HAVSRLIGAP
PGYVGFDQGG LLTEAITKKP HAVLLLDEIE KAHPDIFNIL LQVMDHGTLT DNNGRKTDFR
NVIIVMTTNA GAESLQKRSI GFTDKKEAGD EMADIKRMFT PEFRNRLDSI ISFGALDEEI
ILRVVDKFLM QLEEQLHEKK VEAVFSDTLR KFLSKKGFDP LMGARPMSRL IQDMIRKALA
DELLFGRLVN GGRVTVELDD KDQVKLEFPE GDDPTPPPEE PQEKLEVE
//
