ID A0A0D6EX10_9PROT Unreviewed; 755 AA.
AC A0A0D6EX10;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=ATP-binding protease component {ECO:0000313|EMBL:CEZ20016.1};
GN Name=clpA {ECO:0000313|EMBL:CEZ20016.1};
GN ORFNames=BN1208_1135 {ECO:0000313|EMBL:CEZ20016.1};
OS Candidatus Methylopumilus planktonicus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylopumilus.
OX NCBI_TaxID=1581557 {ECO:0000313|EMBL:CEZ20016.1, ECO:0000313|Proteomes:UP000064007};
RN [1] {ECO:0000313|Proteomes:UP000064007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-10A-171 {ECO:0000313|Proteomes:UP000064007};
RA Salcher M.M.;
RL Submitted (DEC-2014) 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; LN827929; CEZ20016.1; -; Genomic_DNA.
DR RefSeq; WP_046488704.1; NZ_LN827929.1.
DR AlphaFoldDB; A0A0D6EX10; -.
DR STRING; 1581557.BN1208_1135; -.
DR KEGG; mbat:BN1208_1135; -.
DR HOGENOM; CLU_005070_4_2_4; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000064007; Chromosome 1.
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:CEZ20016.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:CEZ20016.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000064007};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 144..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 755 AA; 83594 MW; 38044AD2A02E2289 CRC64;
MIAQELEVSL HMAFMDARQK RHELITVEHL LLAMLDNPSA AEVLKACGSN VEILRNELTQ
YIDEHTPTIS GEDEVDTQPT LGFQRVIQRA MLHVQSSGKK EVNGANVLVA IYGEKDSHAV
YFLHQQGVTR LDVVNFIAHG VSKLNEGETP KPSTEQESDQ ESSSSKALET YTVNLNKMVL
AGKIDPLIGR DSEIERVIQT LCRRRKNNPL LVGEAGVGKT AIAEGLAKRI VDKEVPTILE
GTTIFSLDMG TLLAGTKYRG DFEQRLKSVM KQLNEHKDAI LFIDEIHTLI GAGSASGGTL
DASNLLKPAL SNGTIKCIGA TTYQEYRMVF EKDHALARRF QKIDVNEPSI LDTINILKGL
KTRFEKHHNV KYSVAAIHSA AELSAKYIND RHLPDKAIDV IDEAGAAQRI LPKNKQKKVI
TNKEIEEVVA KIAKIPPKNI SNDDKHALKN LERDLKAVIF GQDKAIENLS SAIKMTRSGL
GVPNKPIGNF LFSGPTGVGK TEVARQLAYI LGIELVRIDM SEYMERHAVS RLIGAPPGYV
GFEQGGLMTE AVNKQPYCVL LLDEIEKAHP DIFNILLQVM DHGSLTDSNG RKTDFRNVTL
IMTTNAGAES LSKTSMGFTQ SKKMGDEQAE IKRLFTPEFR NRLDATVSFA PLSHDVILKV
VDKFLMQLED QLHEKKVDAT FTESLKSYLA KNGFDPSMGA RPMSRLIQDT IRKALADELL
FGKLTNGGNV IIDIDSNDKV KLIFEEENKA ILQES
//
