ID   Y1007_LACLA             Reviewed;         226 AA.
AC   Q9CGT5;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=UPF0758 protein LL1007;
GN   OrderedLocusNames=LL1007; ORFNames=L0306;
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   -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR   EMBL; AE005176; AAK05105.1; -; Genomic_DNA.
DR   PIR; G86750; G86750.
DR   RefSeq; NP_267163.1; NC_002662.1.
DR   RefSeq; WP_003131898.1; NC_002662.1.
DR   AlphaFoldDB; Q9CGT5; -.
DR   SMR; Q9CGT5; -.
DR   STRING; 272623.L0306; -.
DR   PaxDb; Q9CGT5; -.
DR   EnsemblBacteria; AAK05105; AAK05105; L0306.
DR   KEGG; lla:L0306; -.
DR   PATRIC; fig|272623.7.peg.1077; -.
DR   eggNOG; COG2003; Bacteria.
DR   HOGENOM; CLU_073529_0_2_9; -.
DR   OMA; AMPDYEL; -.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd08071; MPN_DUF2466; 1.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR025657; RadC_JAB.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR001405; UPF0758.
DR   InterPro; IPR020891; UPF0758_CS.
DR   PANTHER; PTHR30471; PTHR30471; 1.
DR   Pfam; PF04002; RadC; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   TIGRFAMs; TIGR00608; radc; 1.
DR   PROSITE; PS50249; MPN; 1.
DR   PROSITE; PS01302; UPF0758; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Zinc.
FT   CHAIN           1..226
FT                   /note="UPF0758 protein LL1007"
FT                   /id="PRO_0000190706"
FT   DOMAIN          103..225
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   MOTIF           174..187
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         176
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         187
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   226 AA;  25802 MW;  0436DEAF86CF7801 CRC64;
     MYELKENPYP MQPRERLEFL GEECLSDVEL LAILLRTGTK KYSSLNLALE ILQHFETLDN
     LRKASINELR EISGIGLAKS IEIRAMIEFG KRIQTTNRKR YGQVLSSREY GLSLAFEMQN
     FEQEHLVATY LDGQNRIIEK KTIFIGAVNQ ATASPREILY HAIKNLSVGL LVAHNHPSGN
     LKPSQADKIF TTKIKKSCED VGINFIDHII VGAGNYFSFR EEEIRK