ID A0A0N0J7T5_9PROT Unreviewed; 770 AA.
AC A0A0N0J7T5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:KPF44347.1};
GN Name=clpA {ECO:0000313|EMBL:KPF44347.1};
GN ORFNames=IP80_17915 {ECO:0000313|EMBL:KPF44347.1};
OS beta proteobacterium AAP65.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1523424 {ECO:0000313|EMBL:KPF44347.1, ECO:0000313|Proteomes:UP000037849};
RN [1] {ECO:0000313|EMBL:KPF44347.1, ECO:0000313|Proteomes:UP000037849}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP65 {ECO:0000313|EMBL:KPF44347.1,
RC ECO:0000313|Proteomes:UP000037849};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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:KPF44347.1}.
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DR EMBL; LJHW01000041; KPF44347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0J7T5; -.
DR STRING; 1523424.IP80_17915; -.
DR PATRIC; fig|1523424.3.peg.2997; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000037849; 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:KPF44347.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KPF44347.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037849};
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"
SQ SEQUENCE 770 AA; 84328 MW; AE4640AD5C2BDF58 CRC64;
MIAQELEVSL HMAFVEARQQ RHEFITVEHL LMALLDNPSA AEVLRACAAN IDDLRKSLAT
FIKENTPTVG GTEEVDTQPT LGFQRVIQRA IMHVQSTGSG KKEVTGANVL VAIFGEKDSH
AVYYLHQQGV TRLDVVNFIA HGIKKSDPPE PAKGNEGPQG NEAEKEEGGG DGKGSPLEQF
TQNLNQHALQ GKIDPLIGRE HEVERVIQVL CRRRKNNPLL VGEAGVGKTA IAEGLAWRIT
EKDVPEVLAD ATVYSLDMGA LLAGTKYRGD FEQRLKGVLK QLKDQPNAIL FIDEIHTLIG
AGAASGGTLD ASNLLKPALS SGAMKCIGAT TFTEYRGIFE KDAALSRRFQ KVDVVEPSVE
QTVEILKGLK SRFEEHHSVK YAVGALQAAA ELSAKFINDR HLPDKAIDVI DEAGAAQRIL
PPSKRKKTIT RNEVEEIVAK IARIPPASVS SDDRSKLKTL DRDLKSVVFG QDPAIDALAA
SIKMARSGLG KADKPIGSFL FSGPTGVGKT EVAKQLAYVL GIDLIRFDMS EYMERHAVSR
LIGAPPGYVG FDQGGLLTEA VTKKPHSVLL LDEIEKAHPD VFNVLLQVMD HGSLTDNNGR
KADFRNVMII MTTNAGAETM NKATIGFTNK REQGDEMGDI KRLFTPEFRN RLDAIVNFRA
LDEDIILRVV DKFLLQLESQ LTEKKVEVTF SDALRKHLAK KGFDPLMGAR PMQRLIQDTI
RRALADELLF GRLVDGGRLS VDIDDKDEVQ LDIQPARKSG DKPRAEATPA
//