ID A0A2A2AKQ7_9BURK Unreviewed; 781 AA.
AC A0A2A2AKQ7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:PAT38321.1};
GN Name=clpA {ECO:0000313|EMBL:PAT38321.1};
GN ORFNames=CK625_02185 {ECO:0000313|EMBL:PAT38321.1};
OS Vandammella animalimorsus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Vandammella.
OX NCBI_TaxID=2029117 {ECO:0000313|EMBL:PAT38321.1, ECO:0000313|Proteomes:UP000218054};
RN [1] {ECO:0000313|EMBL:PAT38321.1, ECO:0000313|Proteomes:UP000218054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML00-0135 {ECO:0000313|EMBL:PAT38321.1,
RC ECO:0000313|Proteomes:UP000218054};
RA Bernier A.-M., Bernard K.;
RT "WGS of Clinical strains of the CDC Group NO-1 linked to zoonotic
RT infections in humans.";
RL Submitted (AUG-2017) 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}.
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:PAT38321.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NSJB01000001; PAT38321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2AKQ7; -.
DR Proteomes; UP000218054; 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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:PAT38321.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:PAT38321.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:PAT38321.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218054};
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 149..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 85228 MW; 8E8F9F5589BFAA75 CRC64;
MIAQELEVSL QKAFVEAREK RHEFVTVEHL LLALLDNPSA AEVLRACKAN IEELRSALTG
FIDDNMPQVG GSDEVDTQPT LGFQRVVQRA IMHVQSTGNG KKEVVGANVL VAIFGEKDSH
AAYFLQLQNI TRLDVVNFIA HGIRKDEAGD KAGSADAMGG QEEGQQPGGE RGEKLSPLEQ
YTVNLNQAAA QGRIDPLIGR QQEVERTIQV LCRRRKNNPL LVGEAGVGKT AIAEGLAWRI
TQKDVPEVLE NATVYALDMG ALLAGTKYRG DFEQRLKGVL KSLREKPDAV LFIDEIHTLI
GAGAASGGTL DASNLLKPAL SSGQLKCIGA TTFTEYRGIF EKDAALSRRF QKIDVVEPTV
AETVDILKGL KSRFEEHHSV KYANAALQAA AELSARYIND RQLPDKAIDV IDEAGAAQRI
LAPSKRRKTI GKAEIEEIVA KIARIPPAAV SQDDRSKLKT LERDLKSVVF GQDGALEALA
SAIKMARSGL GKPDKPIGAF LFSGPTGVGK TEAARQLAYI MGIELIRFDM SEYMEPHAVS
RLIGAPPGYV GFDQGGLLTE AVTKKPHAVL LLDEIEKAHP SIYNILLQVM DHGTLTDNNG
RKADFRNVII IMTTNAGAET MNKASIGFTN PRQAGDEMGD IKRMFTPEFR NRLDAIVSFK
PLDEQIILRV VDKFLLQLES QLAEKKVEAS FTDELRKYLA KKGFDPLMGA RPMQRLIQDT
IRKSLADELL FGGLADGGRV LIGLKQVDDG QGGVKDEVQL DITPLKKEAK PKPEEEETAA
E
//