ID A0A1H8E245_9BURK Unreviewed; 780 AA.
AC A0A1H8E245;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:SEN12838.1};
GN ORFNames=SAMN02745977_00513 {ECO:0000313|EMBL:SEN12838.1};
OS Brachymonas denitrificans DSM 15123.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Brachymonas.
OX NCBI_TaxID=1121117 {ECO:0000313|EMBL:SEN12838.1, ECO:0000313|Proteomes:UP000199531};
RN [1] {ECO:0000313|EMBL:SEN12838.1, ECO:0000313|Proteomes:UP000199531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15123 {ECO:0000313|EMBL:SEN12838.1,
RC ECO:0000313|Proteomes:UP000199531};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOCW01000001; SEN12838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8E245; -.
DR STRING; 1121117.SAMN02745977_00513; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199531; 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:SEN12838.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SEN12838.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199531};
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..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 780 AA; 85515 MW; 3D338A4B375A4AFB CRC64;
MIAQELEVTL HMAFVEARQQ RHEFLTVEHL LLALLDNPSA SEVLHACAAN GDDLRTSLGN
FIKDHSPQMP GNDEVDTQPT LGFQRVIQRA IMHVQSTGNG KKEVTGANVL VAIFGEKDSH
AVYYLHQQGV TRLDVVNYIA HGIRKTGESE EPSKPDDSSQ NDGGDEQGGE RNEKASPLEQ
FTNNLNQAAK EGKIDPLIGR DYEVERVIQI LCRRRKNNPL LVGEAGVGKT AIAEGLAWRI
TQGTVPEVLA DAEVYALDMG ALLAGTKYRG DFEQRLKAVL KALKDKPDSV LFIDEIHTLI
GAGAASGGTM DASNLLKPAL SSGQIKCVGA TTFTEYRGIF EKDAALSRRF QKVDVVEPTV
EQTVEILKGL KSRFEEHHSV KYAQAALQAA AELSAKYIND RQLPDKAIDV IDEAGAAQRI
VVASKRKKTI GKAEIEDIVA KIARIPPASV SSDDRGKLAT LERDLKSVVF GQDKALEVLA
SSVKMARSGL GKQDKPIGAF LFSGPTGVGK TEAAKQLAFI MGVELVRFDM SEYMERHAVS
RLIGAPPGYV GFDQGGLLTE QITKKPHSVL LLDEIEKAHP DIFNVLLQVM DHGTLTDNNG
RKADFRNVVI IMTTNAGAET INKSTIGFTN ARQAGDEMAD IKRLFTPEFR NRLDAIVSFK
PLDEQVILRV VDKFLLQLEH QLIEKKVEVT FTDVLRKHLA KKGFDPLMGA RPMQRLIQDT
IRKALADELL FGRLTDGGRL TVDYDEKQEE NNGIVLDIQP LSKKEPKPGT AEPEAKAPVG
//
