Y1515_LACLM
ID Y1515_LACLM Reviewed; 227 AA.
AC A2RLC4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=UPF0758 protein llmg_1515;
GN OrderedLocusNames=llmg_1515;
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 [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 -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR EMBL; AM406671; CAL98091.1; -; Genomic_DNA.
DR RefSeq; WP_011835357.1; NZ_WJVF01000002.1.
DR AlphaFoldDB; A2RLC4; -.
DR SMR; A2RLC4; -.
DR STRING; 416870.llmg_1515; -.
DR EnsemblBacteria; CAL98091; CAL98091; llmg_1515.
DR KEGG; llm:llmg_1515; -.
DR eggNOG; COG2003; Bacteria.
DR HOGENOM; CLU_073529_0_2_9; -.
DR OMA; AMPDYEL; -.
DR PhylomeDB; A2RLC4; -.
DR BioCyc; LLAC416870:LLMG_RS07625-MON; -.
DR Proteomes; UP000000364; 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; Zinc.
FT CHAIN 1..227
FT /note="UPF0758 protein llmg_1515"
FT /id="PRO_1000089818"
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 227 AA; 25872 MW; A6A0B07E64412362 CRC64;
MYELKEKSYP MQPRERLELL GEEYLSDVEL LAILLRTGRK KYSSLNLALE LLQHFGTLDN
FRKASISELK EISGIGQTKA IELRAMIELG KRIQTTTRKR YGQVLSSKEY GMSLAFEMQN
FEQEHLTATY LDGQNQIIEK KTIFIGAFNH ATASPREILY HAVKNLSVGL LVAHNHPSGN
LQPSQADKIF TKKIKNACDN IGINFIDHII VGAGNYYSFR ERDSNLF