Y1318_LISMO
ID Y1318_LISMO Reviewed; 420 AA.
AC Q8Y7G3;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Putative zinc metalloprotease Lmo1318;
DE EC=3.4.24.-;
GN OrderedLocusNames=lmo1318;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR EMBL; AL591978; CAC99396.1; -; Genomic_DNA.
DR PIR; AF1239; AF1239.
DR RefSeq; NP_464843.1; NC_003210.1.
DR RefSeq; WP_003723454.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y7G3; -.
DR SMR; Q8Y7G3; -.
DR STRING; 169963.lmo1318; -.
DR MEROPS; M50.A11; -.
DR PaxDb; Q8Y7G3; -.
DR DNASU; 987698; -.
DR EnsemblBacteria; CAC99396; CAC99396; CAC99396.
DR GeneID; 987698; -.
DR KEGG; lmo:lmo1318; -.
DR PATRIC; fig|169963.11.peg.1355; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_1_0_9; -.
DR OMA; QYMVGFG; -.
DR PhylomeDB; Q8Y7G3; -.
DR BioCyc; LMON169963:LMO1318-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837; PTHR42837; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR TIGRFAMs; TIGR00054; TIGR00054; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..420
FT /note="Putative zinc metalloprotease Lmo1318"
FT /id="PRO_0000088447"
FT TRANSMEM 172..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 176..267
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 420 AA; 46717 MW; 220DD2B8B7C63DCF CRC64;
MTTIIAFIFV FGLIVFFHEL GHFLFAKRAG IMVKDFSIGF GPKIFAYRKK ETQYTIRLLP
IGGYVRMAGE DGEEIELKPG YRVGLELTPE ETVSKIIVNG KDQYVNAQPI EVSLCDLEKE
LFIEGYEDYD DTKKVRYQVE RDALVIDGKI ETMITPYDRS FNAKSLGNRA MTIFAGPLFN
FILAILIFTA LAFVQGGVPS TDNTLGNVLP DGAAAEAGLK KGDEVLSING KETKSWTDIV
QNVSENPGKT LDFKIERDGK TQDIDVKPAT QKENGKDVGK IGVETPMDSS FTAKITNGFT
QTWNWIVQIF TILGNMFTGG FSLDMLNGPV GIYTSTQQVV QYGFMTVLNW TAVLSINLGI
VNLLPLPALD GGRLMFFLYE LVRGKPIDPK KEGIIHFAGF ALLMVLMILV TWNDIQRAFF