ID A0A4S1EGC0_9BURK Unreviewed; 778 AA.
AC A0A4S1EGC0;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:TGV10085.1};
GN Name=clpA {ECO:0000313|EMBL:TGV10085.1};
GN ORFNames=E4695_03440 {ECO:0000313|EMBL:TGV10085.1};
OS Alcaligenaceae bacterium 429.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae.
OX NCBI_TaxID=2562948 {ECO:0000313|EMBL:TGV10085.1, ECO:0000313|Proteomes:UP000306734};
RN [1] {ECO:0000313|EMBL:TGV10085.1, ECO:0000313|Proteomes:UP000306734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=429 {ECO:0000313|EMBL:TGV10085.1,
RC ECO:0000313|Proteomes:UP000306734};
RA Zilliox M.J., Schreckenberger P.C., Putonti C.;
RT "Draft Genome of Alcaligenaceae sp. 429.";
RL Submitted (APR-2019) 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}.
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:TGV10085.1}.
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DR EMBL; SRSN01000022; TGV10085.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4S1EGC0; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000306734; 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:TGV10085.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TGV10085.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000306734};
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..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 84697 MW; 715513CA7C7004B0 CRC64;
MISEELEVSL HMAFVEARAA RHEFITVEHL LLALLDNAAA VEVLRACAAN LETLRQNLKK
FIAENTPIHP GEGDVDTQPT LGFQRVIQRA IMHVSSSGQT KTEVTGANVL VAMYGEKDSH
AVYYLQQQGI SRLDVVNYLS HGIAKSGAAT EPTAQAANKT SGPTDAGAQR STSDAQKSPL
DLYTTNLNAE AGLGRIDPLI GREKEVERVI QVLCRRRKNN PLLVGEAGVG KTAIAEGLAL
RIVQGSVPDL LEDAIVYSLD MGALLAGTKY RGDFEQRLKA VLKDLSEQKQ GILFIDEIHT
LIGAGSASGG TLDASNLLKP ALSSGKLKCM GATTYTEYRG IFEKDHALSR RFQKIDVVEP
TVAETVQILR GLKGHFEAHH GVRYTNAAIA AAAELSARHI TDRFLPDKAI DVIDEAGAAQ
RLLPKSRQKK TIGKQDIQAT VAQIARIPPQ NVSTDDKHKL ATLERDLKSM VFGQSAAIEA
LSSAIKMSRS GLGRPDKPIG SFLFSGPTGV GKTEVARQLA FVLGIELLRF DMSEYMERHA
VSRLIGAPPG YVGFEQGGLL TEAVTKQPHC VLLLDEIEKA HPDIFNILLQ VMDHGTLTDN
NGRKADFRNV ILVMTTNAGA ETLSKSSIGF MKSQSAGDEM ADIKRLFTPE FRNRLDAIVN
FKPLSRDVIL KVVDKFLLQL EHQLNERRVD VVFSDALREH LAANGFDPAM GARPMQRLIQ
DTIRRALADE LLFGRLSDGG QVEVDLDDTG AVVLKFGDTE KPRSEHAQPS DTEAELIG
//