ID A0A1H9JCD3_9PROT Unreviewed; 757 AA.
AC A0A1H9JCD3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:SEQ84468.1};
GN ORFNames=SAMN05421690_100279 {ECO:0000313|EMBL:SEQ84468.1};
OS Nitrosomonas sp. Nm51.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=133720 {ECO:0000313|EMBL:SEQ84468.1, ECO:0000313|Proteomes:UP000198732};
RN [1] {ECO:0000313|EMBL:SEQ84468.1, ECO:0000313|Proteomes:UP000198732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm51 {ECO:0000313|EMBL:SEQ84468.1,
RC ECO:0000313|Proteomes:UP000198732};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOGH01000002; SEQ84468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9JCD3; -.
DR STRING; 133720.SAMN05421690_100279; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000198732; 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:SEQ84468.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SEQ84468.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198732};
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 147..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 757 AA; 84010 MW; 72446EF4BEE45C31 CRC64;
MIAPDLEVSL HMAFVESRQK RHEFITVEHL LLAMLDNASA AEVLNACLVD LEDLRAILID
HISRHTPIIS SDSEVDTQPT LGFQRVIQRA ILHVQSSGKK EVTGANVLVA IFGEKDSHAV
YYLQQRGVTR LDVVNYISHN IRKTPLESEN KTAVENEQEQ GQQDQGPAGN NNMLENYTVN
LNVLALTNKI DPLIGRDQEI ERVIQTLCRR RKNNPLLVGE AGVGKTAIAE GLAKRIVEGD
VPGLLANHQI YALDMGSLLA GTKYRGDFEQ RLKAVLKQLT DNNDTILFVD EIHTLIGAGA
ASGGVLDASN LLKPVLSSGQ LRCIGATTYT EFRGIFEKDH ALSRRFQPID VNEPSVNETV
AILRGLKSRY ELHHDVKYTN SALSLAAELS ERYINDRHLP DKAIDVIDEA GAVQRIMPKS
KKRKVIGKTE IENVVAKIAR IPPQNISAND RNRLKTLERD MKAVVFGQDK AISSLCAAIK
MSRSGLGNPR KPVGSFLFSG PTGVGKTEVA RQLAYTLGIQ LHRFDMSEYM ERHAVSRLIG
APPGYVGFDQ GGLLTETVVK HPYSVLLLDE IEKAHTDIFN ILLQVLDYGT LTDNNGRKAD
FRNVIIIMTT NAGAESLTKT TIGFTKPAHA GDEMAEIKRL FTPEFRNRID AIISFLALNE
DVILQVTDKF LMQLEAQLQE KKVETTFTER LCKFLAKNGF DPLMGARPME RLIQDTIRRA
LADELLFGRL INGGKVTVDI DHSDKIQLVF EEEAVEA
//