ID   CLPL_LACLL              Reviewed;         763 AA.
AC   Q06716;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpL;
GN   Name=clpL;
OS   Lactococcus lactis subsp. lactis (Streptococcus lactis).
OG   Plasmid pUCL22.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CNRZ 270;
RX   PubMed=8387149; DOI=10.1111/j.1365-2958.1993.tb01187.x;
RA   Huang D.C., Huang X.F., Novel G., Novel M.;
RT   "Two genes present on a transposon-like structure in Lactococcus lactis are
RT   involved in a Clp-family proteolytic activity.";
RL   Mol. Microbiol. 7:957-965(1993).
CC   -!- FUNCTION: Could be the ATP-dependent specificity component of an ATP-
CC       dependent protease.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR   EMBL; X62333; CAA44207.1; -; Genomic_DNA.
DR   PIR; S35908; S35908.
DR   AlphaFoldDB; Q06716; -.
DR   SMR; Q06716; -.
DR   MEROPS; X20.001; -.
DR   PRIDE; Q06716; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
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; SSF52540; SSF52540; 2.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Plasmid; Repeat.
FT   CHAIN           1..763
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpL"
FT                   /id="PRO_0000191233"
FT   REGION          136..386
FT                   /note="I"
FT   REGION          437..629
FT                   /note="II"
FT   BINDING         181..188
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         511..518
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   763 AA;  86019 MW;  E92CCF2F629D9C14 CRC64;
     MKLISLLFKQ ISVVILIDSI STLPSDTEKL CYNSVIVLKL SWSLTLHIQI FMEVWQYGKF
     QWNDPFFNND MDDVFNQLFR RMDNQNSEVR GISLMDNRCH RMSLLNTEQL ASYPKIIKQW
     KYLKMVNRLL KKEGFIEKLG TNLTEQARDG LLDPVIDREN EIQKPAQKFC RRRKKNPLLV
     GESGVGKTAV VEGLAQRIVA GKVPETIQDK EIYSIDLSSL EAGTQYRGSF EENIKQLVEE
     VKAAGNIILF IDEIHQILGT GALAGEEVKG LADIIKPLLC HVAKLSVIGA TTQDEYRNTI
     LKNAALARRF NDVVINEPTA ADTLRILQGI KELYEKHHHV VLPDDEKKAA VDYSIKYIHN
     RHLPDKAIDL IDDCGSFSGK NSQTDVETLD QRLKNKRQLR RPAIKSEDFA KAADIKRVDR
     GTKQKIKKTH QKEKITATID DVAQSVERLT GIPVSDMGAN DIEHLKNLDK RLKVMVIGED
     EAVKMVAKAI RRNRAGFSEG DQPKGSFLFV GPTGVGKTEL SQALALDMFG NENALFGIDM
     SEYADRTAVS KLIGTSAGYV GYEDNANTLT ERVRRNPYSV ILLDEIEKAD PQVLTLLLQV
     MDDGRLTDGQ GSVIDFRNTI IIMTSNAGFG NEALSGDKQR VQSLMDKLAP FFAQNFRPEF
     RNRLDNIVEF SHLTKQDLSQ IVDLMLADVQ KTLAKKSIKL EVTKAAKDWL MEQGYDEAMG
     ARPLRRVIEQ QIRDKVTDFY LDHLDVKNLK ADLVDAEIVI SAA