ID A0A4P6ZJA4_9LACO Unreviewed; 833 AA.
AC A0A4P6ZJA4;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:QBP17815.1};
GN ORFNames=ELX58_01270 {ECO:0000313|EMBL:QBP17815.1};
OS Acetilactobacillus jinshanensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Acetilactobacillus.
OX NCBI_TaxID=1720083 {ECO:0000313|EMBL:QBP17815.1, ECO:0000313|Proteomes:UP000294321};
RN [1] {ECO:0000313|Proteomes:UP000294321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HSLZ-75 {ECO:0000313|Proteomes:UP000294321};
RA Jian Y., Xin L., Hong Z.J., Ming L.Z., Hong X.Z.;
RT "A new species of lactobacillus.";
RL Submitted (DEC-2018) 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}.
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DR EMBL; CP034726; QBP17815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P6ZJA4; -.
DR KEGG; lji:ELX58_01270; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000294321; Chromosome.
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: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 Gene3D; 4.10.860.10; UVR domain; 1.
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; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
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; PS50151; UVR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:QBP17815.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:QBP17815.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:QBP17815.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000294321};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 423..458
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
SQ SEQUENCE 833 AA; 92987 MW; 22D6754AB70ACF89 CRC64;
MDNLFTPSAR NVLVISQKEA KRFRHQAIGT EHLLLALSME KNGIAYHALR QFSITDADIR
GEIEHFTGYG TLAGMGPETY LPYSPKAKLI LSIAAKIARQ YGAEKVGTEH LLLALLSDNT
ILSSRILIAL GVKPEDVKTV TLRKMGVSSI SAQRMALNHR RSRRRQDTPT LNSLATDLTK
EAREGRLDPV IGRDREIQRV IQILSRRTKN NPVLLGNPGV GKTAIAEGLA ERIVNGDVPS
DMAHKRLMSL DMGSLVAGTK YRGEFENRLR HIINEIKTDG HVILFVDELH TLVGAGGAEG
AIDASNILKP SLARGDFQLM GATTLAEYRK HIEPDAALER RFATITVKEP TKDQTFKILQ
GLRLKYEKFH HVNITDAALK TAVRLSTRYI PDRFLPDKAI DLMDEAAAMI RVNQRPNKVS
KNRRRYLKLA KAKETAIESQ HFEKAAQIRN HQLALKDQMR LSEKKEKLAK RDLKPGQYSL
KETPDDIAKV VSEWTGVPVT RLTKSAKDRL LNLEKILHKR IIGQDEAVDS VSKAIRRARS
GLKDPNRPIG SFMFLGPTGV GKTQLAKELA KTVFGSEKDL IRIDMGEYME KYSTSRLIGS
APGYVGYSQG GQLTDKVRTH PYSVVLFDEV EKANPDVFNV ILQLLDEGYL TDTKGRKVDF
RNTIIIMTSN LGATTLRDAK PVGFGNEKQK ISYEDMSDTI KHQLKEHFRP EFINRIDDII
IFHSLTKPQI RKIVKLMASD LLKRVIAKHI QIKMTPAAVN LIATKGYKPA YGARPIRRVL
QNLVEDPLSD DLLSGKVASG DAVTIGARQG KITISSKPIK KSPKTKRSKV ADH
//