ID   A0A0B7J169_9PROT        Unreviewed;       764 AA.
AC   A0A0B7J169;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=ATP-binding protease component {ECO:0000313|EMBL:CEN56508.1};
GN   Name=clpA {ECO:0000313|EMBL:CEN56508.1};
GN   ORFNames=BN1209_1471 {ECO:0000313|EMBL:CEN56508.1};
OS   Candidatus Methylopumilus turicensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylopumilus.
OX   NCBI_TaxID=1581680 {ECO:0000313|EMBL:CEN56508.1, ECO:0000313|Proteomes:UP000056322};
RN   [1] {ECO:0000313|Proteomes:UP000056322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMS-10A-171 {ECO:0000313|Proteomes:UP000056322};
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; LN794158; CEN56508.1; -; Genomic_DNA.
DR   RefSeq; WP_045751591.1; NZ_LN794158.1.
DR   AlphaFoldDB; A0A0B7J169; -.
DR   STRING; 1581680.BN1209_1471; -.
DR   KEGG; mbac:BN1209_1471; -.
DR   HOGENOM; CLU_005070_4_2_4; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000056322; 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:CEN56508.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:CEN56508.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000056322};
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"
SQ   SEQUENCE   764 AA;  84003 MW;  3D2CAAF4791C7D13 CRC64;
     MIAQELEVSL HMVFMDARQK RHELITVEHL LVAMIDNPTA ADVLRACGAN LDNLRSELNH
     YIEEHTPMVG GDEEVDTQPT LGFQRVIQRA ILHVQSSGKK EVTGANVLVA IYGEKDSHAV
     FFLQQQGITR LDVVNYISHG VAKMAEEAKR ADTDQAADTE APPASALDSY TLNLNEQVLA
     GKIDPVIGRD KELERVIQTL CRRRKNNPLL VGEAGVGKTA IAEGLARRIV EKSVPEVLAN
     AVIYSLDMGA LLAGTKYRGD FEQRLKAVMK KLEEQPDAVL FIDEIHTLIG AGAASGGTLD
     ASNLLKPALS NGSLKCIGAT TYQEYRGIFE KDHALSRRFQ KVDVEEPSIA ETVQILKGLK
     SRFEKHHSVK YTLGALNTAA ELSAKYINDR HLPDKAIDVI DEAGAAQRIL PKSKQKKVIG
     DKEIEDIIAK IARIPPKNIS SDDRNALKTL DRDLKAVVFG QDKAIESLAS AIKMARSGLG
     SQNKPIGSFL FSGPTGVGKT EVAKQLAYTL GIELVRFDMS EYMERHAVSR LIGAPPGYVG
     FEQGGLMTEA ITKHPYCVLL LDEIEKAHPD IYNILLQVMD HGTLTDNNGR KADFRNVTII
     MTTNAGAESL SKTTIGFTQG KQAGDEMAEI KRLFSPEFRN RLDATVSFAP LSQEIIMRVV
     DKFLMQLEDQ LHEKKVEANF SDKLKAYLGK KGFDPLMGAR PMSRLIQDTI RRGLADELLF
     GKLANGGHVF VDIDDKDQIT LDFEDIASDK SVGNSDQQTA DLTD
//