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 27-MAR-2024, entry version 122.
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; Bacillota; 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 PaxDb; 272623-L0221; -.
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 OrthoDB; 9803641at2; -.
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 CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
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; 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 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; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF46600; C-terminal UvrC-binding domain of UvrB; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//
