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Database: UniProt
Entry: F9UMJ6_LACPL
LinkDB: F9UMJ6_LACPL
Original site: F9UMJ6_LACPL 
ID   F9UMJ6_LACPL            Unreviewed;       837 AA.
AC   F9UMJ6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=ATP-dependent Clp protease, ATP-binding subunit ClpC {ECO:0000313|EMBL:CCC78435.1};
GN   Name=clpC {ECO:0000313|EMBL:CCC78435.1};
GN   OrderedLocusNames=lp_1019 {ECO:0000313|EMBL:CCC78435.1};
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668 {ECO:0000313|EMBL:CCC78435.1, ECO:0000313|Proteomes:UP000000432};
RN   [1] {ECO:0000313|EMBL:CCC78435.1, ECO:0000313|Proteomes:UP000000432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1
RC   {ECO:0000313|Proteomes:UP000000432};
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W., Stiekema W.,
RA   Lankhorst R.M., Bron P.A., Hoffer S.M., Groot M.N., Kerkhoven R.,
RA   de Vries M., Ursing B., de Vos W.M., Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WCFS1;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.F.T.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CCC78435.1, ECO:0000313|Proteomes:UP000000432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1
RC   {ECO:0000313|Proteomes:UP000000432};
RX   PubMed=22156394; DOI=10.1128/JB.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.F.T.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
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}.
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DR   EMBL; AL935263; CCC78435.1; -; Genomic_DNA.
DR   RefSeq; WP_011101242.1; NC_004567.2.
DR   RefSeq; YP_004888949.1; NC_004567.2.
DR   AlphaFoldDB; F9UMJ6; -.
DR   STRING; 220668.lp_1019; -.
DR   EnsemblBacteria; CCC78435; CCC78435; lp_1019.
DR   KEGG; lpl:lp_1019; -.
DR   PATRIC; fig|220668.9.peg.861; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_9; -.
DR   OrthoDB; 9803641at2; -.
DR   PhylomeDB; F9UMJ6; -.
DR   Proteomes; UP000000432; 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; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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:CCC78435.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:CCC78435.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000432};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          426..461
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          153..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          422..468
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   837 AA;  92657 MW;  E2AE3B4941C39811 CRC64;
     MDNLFTPSAK SVLVLAQEQA KYFKHQAVGT EHLLLALAIE KNGIANKVLQ QYAVSEDDIR
     EEIERFTGYG TLSNVGKDTY LPYSPKAKEI LSVAGDEAKR LGANKIGTEH LLLAMLSDES
     ILSSRILMNL NLDLGQTRKV VLRKLGVSDA MSKRKGNAAN RGGKKTEGTP TLDSLARDLT
     QLASEQEMDP VVGRSKEVKR VIQILSRRTK NNPVLIGEPG VGKTAIAEGL AQKIVAGDVP
     TDMADKRLMM LDMGSLVAGT KYRGEFEDRL KKVIDEIYND GHVILFIDEL HTLIGAGGAE
     GAIDASNILK PALARGELQT IGATTLNEYQ KYIESDAALE RRFATVMVNE PTEDEAVEIL
     DGLRPRYEEH HRVTITDEAV DQAVKLSSRY ISDRFLPDKA IDLMDEAAAK VRIDQMDQPT
     KLSKNQDKLA QLREDKETAI EAQDFEQAAD IRKQEMQLKQ RLDRIEADQD AEVTEGATPH
     YDLQVTGEDI AQVVAEWTGV PLTQLQKSES ERLVNLEKIL HERVVGQPEA VSAVARAIRR
     ARSGLKDPSR PIGSFMFLGP TGVGKTELAK ALAAAMFGSE DNMIRIDMSE YMERYSTSRL
     IGSAPGYVGY DEGGQLTEKV RQKPYSVVLF DEVEKAHPDV FNILLQVLDD GYLTDSKGRK
     VDFRNTILIM TSNLGATTLR DEKSVGFGAT DKANDYNAVA ATIRATLKQT FRPEFLNRID
     ETIVFHSLNK EELHEIVKLM SQEIVDRVAQ QGIKIKITPA AIDVVAKAGF DPEYGARPIR
     RALQTEIEDR LSEELLTGAI KVDDQVTIGA SKGTITINIK TSLRQMVVRP FLQSRRD
//
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