ID Q0AEG1_NITEC Unreviewed; 756 AA.
AC Q0AEG1;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:ABI60271.1};
DE EC=3.4.21.92 {ECO:0000313|EMBL:ABI60271.1};
GN OrderedLocusNames=Neut_2048 {ECO:0000313|EMBL:ABI60271.1};
OS Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=335283 {ECO:0000313|EMBL:ABI60271.1, ECO:0000313|Proteomes:UP000001966};
RN [1] {ECO:0000313|EMBL:ABI60271.1, ECO:0000313|Proteomes:UP000001966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101675 / C91 / Nm57 {ECO:0000313|Proteomes:UP000001966};
RX PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x;
RA Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S.,
RA Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.;
RT "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas
RT eutropha C91: implications for niche adaptation.";
RL Environ. Microbiol. 9:2993-3007(2007).
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; CP000450; ABI60271.1; -; Genomic_DNA.
DR RefSeq; WP_011635068.1; NC_008344.1.
DR AlphaFoldDB; Q0AEG1; -.
DR STRING; 335283.Neut_2048; -.
DR KEGG; net:Neut_2048; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_4; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000001966; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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:ABI60271.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ABI60271.1};
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..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 756 AA; 83344 MW; 85285C6829F89EE7 CRC64;
MIAQELEVSL HMAFVESRQK RHEFITVEHL LLALLDNPSA IKVLLACTVD IEDLRKSLQD
HIARHTPVVE GSGDVDTQPT LGFQRVIQRA ILHVQSSGKK EVTGANVLVA IFGEKDSHAV
YFLQQKGATR LDVVNYISHK IDKTAQNSES EKNEDSTDSE QRDSGSPLES YTINLNSQAA
ANRIDPLIGR EKEVERVIQT LCRRRKNNPL LVGEAGVGKT AIAEGLARRI TENRVPDVLA
NHQVYALDMG ALLAGTKYRG DFEQRLKAVL KQLTDNPKAI LFIDEIHTLI GAGAASGGTL
DASNLLKPAL SSGQLKCIGA TTYNEYRGIF EKDHALSRRF QKIDISEPDI SETVEILRGL
KSRYEKHHNV RYTEVALTAA AELSARFIND RHLPDKAIDV IDEAGAAQRV LPKSRQRKII
GKQEIEHVIA GIARIPPQNV SNDDRNKLKT LDRDLKAIVF GQDAAIDALT AAIKMARSGL
GNTGKPIGSF LFSGPTGVGK TEVARQLAYI LGIPLHRFDM SEYMERHAVS RLVGAPPGYV
GFDQGGLLTE TIIKQPHAVL LFDEIEKAHP DIFNVMLQIM DYGTLTDNNG RKADFRNVII
IMTTNAGADT LTKTVIGFTK HAKSGDEMIE IKRLFTPEFR NRLDAIISFA PLGEAIILRV
VDKFLIELEA QLQEKKVDVT FTDNLRSHLA SHGFDPLMGA RPMARLIQDI IRRALADELL
FGQLVNGGKV TVDIGEDGKA VLTFENKENV AAPIPS
//
