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
//