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Database: UniProt
Entry: X0PBW4_9LACO
LinkDB: X0PBW4_9LACO
Original site: X0PBW4_9LACO 
ID   X0PBW4_9LACO            Unreviewed;       831 AA.
AC   X0PBW4;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=ATP-binding Clp protease subunit {ECO:0000313|EMBL:KRM04430.1};
DE   SubName: Full=ATP-dependent Clp protease, ATP-binding subunit ClpC {ECO:0000313|EMBL:GAF37543.1};
GN   ORFNames=FD41_GL000840 {ECO:0000313|EMBL:KRM04430.1}, JCM14108_2583
GN   {ECO:0000313|EMBL:GAF37543.1};
OS   Lentilactobacillus farraginis DSM 18382 = JCM 14108.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lentilactobacillus.
OX   NCBI_TaxID=1423743 {ECO:0000313|EMBL:GAF37543.1, ECO:0000313|Proteomes:UP000019488};
RN   [1] {ECO:0000313|EMBL:GAF37543.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14108 {ECO:0000313|EMBL:GAF37543.1};
RA   Yuki M., Oshima K., Suda W., Kitahara M., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequences of Two Lactobacillus Strains, L. farraginis JCM
RT   14108T and L. composti JCM 14202T, Isolated from Compost of Distilled
RT   Shochu Residue.";
RL   Genome Announc. 2:e00257-14(2014).
RN   [2] {ECO:0000313|EMBL:KRM04430.1, ECO:0000313|Proteomes:UP000051966}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18382 {ECO:0000313|EMBL:KRM04430.1,
RC   ECO:0000313|Proteomes:UP000051966};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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|RuleBase:RU004432}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAF37543.1}.
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DR   EMBL; BAKI01000037; GAF37543.1; -; Genomic_DNA.
DR   EMBL; AZFY01000119; KRM04430.1; -; Genomic_DNA.
DR   RefSeq; WP_035180779.1; NZ_BAKI01000037.1.
DR   AlphaFoldDB; X0PBW4; -.
DR   STRING; 1423743.FD41_GL000840; -.
DR   PATRIC; fig|1423743.5.peg.866; -.
DR   eggNOG; COG0542; Bacteria.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000019488; Unassembled WGS sequence.
DR   Proteomes; UP000051966; 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: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; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
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; 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:GAF37543.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:GAF37543.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..150
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          151..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          461..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   831 AA;  92178 MW;  FDAD60FD6E4D8E7B CRC64;
     MNNLFTPSAK NVLTIAQEQA KKFKHQAIGT EHLLLGLLIE TNGIAYKALQ QFSVTAEDIT
     EEVERFAGYG NLKDLSSNDY LPYSPKAKEV LAQAGEFAKK NGVPKVGTEH ILLSLLTDET
     ILSSRILINL GLDLSQIRKV TLRKMGISGG SMASNMATNK RGARPSKQKD SKTPTIDSLA
     RDLTEMAREN RLDPTIGRDL EVKRVVQILA RRTKNNPVLI GEPGVGKTAI AEGLAERIVN
     GDVPGDMVNK RLMMLDMGSL VAGTKYRGEF EDRLKKVIEE IYQDGNIILF IDELHTLIGA
     GGAEGAIDAS NILKPALARG ELQLIGATTL DEYQKYIESD AALERRFAKV MVDEPTSDET
     VQILKGLRPK YEQHHHVEIT DEAIQTAVNL SNRYISDRFL PDKAIDLMDE AAAKVRIDHL
     QNSDVVDDHK ELSDLLDQLN EALVAQDYEK ASKIRKQANK LQDTLTKQDE APEDDNDAHY
     PVKETSQDIA QIVAEWTGIP VTRLSKSEAD RLVNLESVLH QRVVGQEEAI SAVSRSIRRA
     RSGLKDPNRP IGSFMFLGPT GVGKTELAKA VAEAVFGSEE DMIRVDMSEY MEKYSTSRLI
     GSAPGYVGYD EGGQLTEKVR QKPYSVVLFD EVEKAHPDVF NLLLQVLDDG YLTDSKGRKI
     DFRNTVIIMT SNLGATTLRD KKTVGFGQED TKEDYGAMKD TIKAALKQRF RPEFLNRIDE
     VVIFHSLTKA ELDQIVKLMT KPVIKRIHDQ GIDIKVTKTA IGIISKVGFD PQYGARPIRR
     AIQTELEDNL SAKLLSKEIV PGDSVTVGGR NNQITISVKK PNRQTLVDNK K
//
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