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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
 
 
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