ID   CLPE_LACLA              Reviewed;         748 AA.
AC   Q9CI09;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpE;
GN   Name=clpE; OrderedLocusNames=LL0557; ORFNames=L0221;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
CC   -!- FUNCTION: Could be necessary for degrading proteins generated by
CC       certain types of stress. {ECO:0000250}.
CC   -!- INDUCTION: By heat shock. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. ClpE subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE005176; AAK04655.1; -; Genomic_DNA.
DR   PIR; E86694; E86694.
DR   RefSeq; NP_266713.1; NC_002662.1.
DR   RefSeq; WP_003130823.1; NC_002662.1.
DR   AlphaFoldDB; Q9CI09; -.
DR   SMR; Q9CI09; -.
DR   STRING; 272623.L0221; -.
DR   PaxDb; Q9CI09; -.
DR   EnsemblBacteria; AAK04655; AAK04655; L0221.
DR   KEGG; lla:L0221; -.
DR   PATRIC; fig|272623.7.peg.595; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_3_9; -.
DR   OMA; ERMKAVM; -.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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   InterPro; IPR036876; UVR_dom_sf.
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; SSF46600; SSF46600; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
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; Chaperone; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Repeat; Stress response; Zinc; Zinc-finger.
FT   CHAIN           1..748
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpE"
FT                   /id="PRO_0000191225"
FT   DOMAIN          359..394
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT   ZN_FING         3..32
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
FT   REGION          74..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          107..354
FT                   /note="I"
FT   REGION          407..598
FT                   /note="II"
FT   COMPBIAS        74..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         152..159
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         481..488
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   748 AA;  83145 MW;  738ECF1B994B31B7 CRC64;
     MLCQNCNINE ATIHLYTSVN GQKKQIDLCQ NCYQIMKSGG QEALFGAGNA SNGNSDEPFN
     PFNDIFSALH GQDFNGAAST QTPPTQTGGR GPRGPQNPRA KQPKGMLEEF GINITESARR
     GEIDPVIGRD EEIKRVIEIL NRRTKNNPVL IGEPGVGKTA VVEGLAQKIV DGDVPQKLQN
     KEVIRLDVVS LVQGTGIRGQ FEERMQKLMD EIRKRNDVIM FIDEIHEIVG AGSAGDGNMD
     AGNILKPALA RGELQLVGAT TLNEYRIIEK DAALERRMQP VKVDEPSVDE TITILRGIQA
     RYEDYHHVKY TDEAIEAAAH LSNRYIQDRF LPDKAIDLLD ESGSKKNLTL KFVDPEDINR
     RIADAETKKN EATQAEDFEK AAHFRDQITK LRELQNHEVS DDEIPVITEK DIEQIVEQKT
     HIPVGDLKEK EQTQLINLAD DLKAHVIGQD EAVDKIAKAI RRSRVGLGKP NRPIGSFLFV
     GPTGVGKTEL AKQLAKELFG SSESMIRFDM SEYMEKHSVA KLIGAPPGYV GYEEAGQLTE
     RVRRNPYSLI LLDEIEKAHP DVMHMFLQIL EDGRLTDAQG RTVSFKDSLI IMTSNAGTGK
     VEASVGFGAA REGRTKSVLG QLGDFFSPEF MNRFDGIIEF SALSKENLLK IVDLMLDEVN
     EQIGRNDIHL SVTQAAKEKL VDLGYNPAMG ARPLRRTIQE NIEDSIADFY IEHPEYKELV
     ADLIDDKIVI SNQAQETAET TDEEVPAE