ID   CLPE_LACLM              Reviewed;         748 AA.
AC   Q9S5Z2; A2RIN7;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpE;
GN   Name=clpE; OrderedLocusNames=llmg_0528;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=10094684; DOI=10.1128/jb.181.7.2075-2083.1999;
RA   Ingmer H., Vogensen F.K., Hammer K., Kilstrup M.;
RT   "Disruption and analysis of the clpB, clpC, and clpE genes in Lactococcus
RT   lactis: clpE, a new Clp family in Gram-positive bacteria.";
RL   J. Bacteriol. 181:2075-2083(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
CC   -!- FUNCTION: Along with ClpP could be necessary for degrading proteins
CC       generated by certain types of stress.
CC   -!- INDUCTION: By heat shock.
CC   -!- MISCELLANEOUS: Disruption of ClpE reduces tolerance for puromycin.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. ClpE subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF023421; AAD01782.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL97132.1; -; Genomic_DNA.
DR   RefSeq; WP_011834563.1; NZ_WJVF01000027.1.
DR   AlphaFoldDB; Q9S5Z2; -.
DR   SMR; Q9S5Z2; -.
DR   STRING; 416870.llmg_0528; -.
DR   EnsemblBacteria; CAL97132; CAL97132; llmg_0528.
DR   KEGG; llm:llmg_0528; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_3_9; -.
DR   OMA; ERMKAVM; -.
DR   PhylomeDB; Q9S5Z2; -.
DR   BioCyc; LLAC416870:LLMG_RS02775-MON; -.
DR   Proteomes; UP000000364; 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   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Metal-binding; Nucleotide-binding; Repeat;
KW   Stress response; Zinc; Zinc-finger.
FT   CHAIN           1..748
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpE"
FT                   /id="PRO_0000191226"
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..104
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"
FT   CONFLICT        476
FT                   /note="S -> F (in Ref. 1; AAD01782)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   748 AA;  83206 MW;  EF5F14E3211AA94A CRC64;
     MLCQNCNINE ATIHLYTSVN GQKKQIDLCQ NCYQIMKSGG QEALFGAGNA SNGNSDEPFN
     PFNDIFSALQ GQDFNGAASN 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
     RIADAESKKN EATKAEDFEK AAHFRDQISK LRELQKQEVT DEDMPVITEK DIEQIVEQKT
     QIPVGDLKEK EQTQLINLAD DLKAHVIGQD EAVDKISKAI RRSRVGLGKP NRPIGSFLFV
     GPTGVGKTEL AKQLAKELFG SSESMIRFDM SEYMEKHSVA KLIGAPPGYV GYEEAGQLTE
     RVRRNPYSLI LLDEIEKAHP DVMHMFLQIL EDGRLTDAQG RTVSFKDSLI IMTSNAGTGK
     VEASVGFGAA REGRTKSVLG QLGDFFSPEF MNRFDGIIEF SALSKENLLK IVDLMLDEVN
     EQIGRNDIHL SVTQAAKEKL VDLGYNPAMG ARPLRRIIQE NIEDSIADFY IEHPEYKQLV
     ADLIDDKIVI SNQTQETAET TDEEVPAE