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Database: UniProt
Entry: A0A4P6ZJA4_9LACO
LinkDB: A0A4P6ZJA4_9LACO
Original site: A0A4P6ZJA4_9LACO 
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
//
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