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Database: UniProt
Entry: A0A0N0J7T5_9PROT
LinkDB: A0A0N0J7T5_9PROT
Original site: A0A0N0J7T5_9PROT 
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
//
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