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Database: UniProt
Entry: A0A2A2AKQ7_9BURK
LinkDB: A0A2A2AKQ7_9BURK
Original site: A0A2A2AKQ7_9BURK 
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}.
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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
//
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