ID A0A0C1LXF8_9LACO Unreviewed; 830 AA.
AC A0A0C1LXF8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=ATP-dependent Clp protease, ATP-binding subunit ClpC {ECO:0000313|EMBL:KID41405.1};
GN ORFNames=LfDm3_1071 {ECO:0000313|EMBL:KID41405.1};
OS Fructilactobacillus fructivorans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Fructilactobacillus.
OX NCBI_TaxID=1614 {ECO:0000313|EMBL:KID41405.1, ECO:0000313|Proteomes:UP000031397};
RN [1] {ECO:0000313|EMBL:KID41405.1, ECO:0000313|Proteomes:UP000031397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DmCS_002 {ECO:0000313|EMBL:KID41405.1,
RC ECO:0000313|Proteomes:UP000031397};
RA Newell P.D., Chaston J.M., Douglas A.E.;
RT "Functional and comparative genomic analyses of the Drosophila gut
RT microbiota identify candidate symbiosis factors.";
RL Submitted (JUN-2014) 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}.
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:KID41405.1}.
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DR EMBL; JOJZ01000020; KID41405.1; -; Genomic_DNA.
DR RefSeq; WP_039144795.1; NZ_RIHD01000002.1.
DR AlphaFoldDB; A0A0C1LXF8; -.
DR GeneID; 74913733; -.
DR PATRIC; fig|1614.7.peg.1018; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000031397; 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 InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF193; CHAPERONE PROTEIN CLPB; 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.
DR PROSITE; PS50151; UVR; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:KID41405.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KID41405.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031397};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 423..458
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 147..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 419..472
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 149..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 830 AA; 92244 MW; 3269CE23E34ABB83 CRC64;
MHNLFTPSAK NVLVIAQEQA KSFQHQAVGT EHMLLALTIE KNGIAYQTLQ QLAVSEADVR
EEIEQLAGYG NLKVDGNTYL PYSPKMKEIL ALAGKIAKQY GATKVGTEHI LLALTSDDAM
LSSRILTNLG VSPEQVRKVT IRKMGVADTN MASDTNSNND SEQSDTPTLD SLARDLTKAA
RDNQLDPVVG RTSEVRRVIQ VLSRRTKNNP VLIGEPGVGK TAIAEGLAEK IVGKSVPSDM
QNKRVMELDM GSLVAGTKYR GQFEDRLKKV LKEVEDSGNV ILFIDELHTL IGAGGTEGSV
DASNILKPSL ARGQVQVMGA TTLDEYQKYI ESDEALERRF ATVEIEEPSK DESRKILKGL
RPKYEEHHHV QITDDAINAA VDLSSRYISN RYLPDKAIDL MDEGAAKVRL DSTGKDDKLA
NAESKLSSVK NDKDKAIEEQ RFEDAVSIRK QEQKLQKEIA DLTQKQRIKE NDANKTHNYR
LKENAEDIAQ IVSEWTGIPV THLKQSDKKR LVNLEKILHE RVVGQDEAVS AVARAIRRAR
SGLKDPNRPI GSFMFLGPTG VGKTELAKDL AEAMFGSEDD MIRVDMSEFM EKYSTSRMVG
SAPGYVGYDE GGQLTEKVRK HPYSVVLLDE VEKAHPDVFN LLLQVLDDGY LTDAKGRKVD
FRNTVIIMTS NIGATELQYK NTVGFAAEKS DDDYAAMKAT IQDQLKKFFK PEFLNRIDDT
VVFHSLTKSE LHRIVKLMSQ DLLNRADGMG YKVRMTPASI DLVAEVGYNP TYGARPIRRA
LQDKVEDPLS EDLLAGKFKP GDHITIGAHK NKITINKRDV KNPKEEILSK
//
