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Database: UniProt
Entry: A0A1H9JCD3_9PROT
LinkDB: A0A1H9JCD3_9PROT
Original site: A0A1H9JCD3_9PROT 
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}.
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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
//
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