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Database: UniProt
Entry: A0A142LIA4_9PROT
LinkDB: A0A142LIA4_9PROT
Original site: A0A142LIA4_9PROT 
ID   A0A142LIA4_9PROT        Unreviewed;       755 AA.
AC   A0A142LIA4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Clp protease ClpX {ECO:0000313|EMBL:AMS31950.1};
GN   Name=clpA {ECO:0000313|EMBL:AMS31950.1};
GN   ORFNames=AEM42_05180 {ECO:0000313|EMBL:AMS31950.1};
OS   Betaproteobacteria bacterium UKL13-2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1690485 {ECO:0000313|EMBL:AMS31950.1, ECO:0000313|Proteomes:UP000075227};
RN   [1] {ECO:0000313|Proteomes:UP000075227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Driscoll C.B.;
RL   Submitted (JUL-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}.
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DR   EMBL; CP012157; AMS31950.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A142LIA4; -.
DR   STRING; 1690485.AEM42_05180; -.
DR   KEGG; beb:AEM42_05180; -.
DR   PATRIC; fig|1690485.4.peg.1170; -.
DR   Proteomes; UP000075227; Chromosome.
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:AMS31950.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AMS31950.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075227};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          144..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   755 AA;  82780 MW;  50667851D810D9D2 CRC64;
     MIAHELEMSL HAAFVEARHK RHEFITVEHL LLALLDNPSA QEVLKACAAK VDDLRKSLTE
     FIEQHTPIVA GDEEVNTQPT LGFQRVIQRA ILHVQSSGKK EVMGANVMVA IYGEKDSHAV
     YYLHQQGVSR LDVVNFISHG ISKAAPQGGE KAETESETAE GEQAGGALDQ FTQNLNQSAI
     DGKIDPLIGR EHEVERVIQI LCRRRKNNPL LVGEAGVGKT AIAEGLAKRI VDGEVPEILA
     KSQVYALDMG SLLAGTKYRG DFEQRLKAVL KQLYDNPNAI LFIDEIHTLI GAGSASGGTL
     DASNLLKPAL SSGQLKCIGA TTYQEFRGVF EKDHALSRRF QKIDVNEPSV SETIEILKGL
     KSRFETHHNV KYTSTALTTA AELAAKYIND RHLPDKAIDV IDEAGAAQRI APKSKQKKTI
     GKSEIEEIIA KIARIPARNV SSNDRNALKT LDRDLKSVVF GQDKAIEALS AAIKMARSGL
     GSTTKPIGSF LFSGPTGVGK TEVAKQLAFI LGVELIRFDM SEYMERHAVS RLIGAPPGYV
     GFDQGGLMTE AITKQPYSVL LLDEIEKAHP DIYNVLLQVM DHGTLTDNNG RKADFRNVVI
     IMTTNAGASE LSKTSIGFTN DKKAGDEIAE IKRMFTPEFR NRLDATISFA PLNEQIILQV
     VDKFLMQLEA QLSEKKVDVT FTETLKKYLA KNGFDPQMGA RPMSRLIQDT IRRALADELL
     FGKLASGGRV TIDMGPDDKV KLDISEEKEP QPAES
//
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