Y2128_LACLA
ID Y2128_LACLA Reviewed; 428 AA.
AC Q9CDT3;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Putative zinc metalloprotease LL2128;
DE EC=3.4.24.-;
GN OrderedLocusNames=LL2128; ORFNames=L181494;
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 -!- 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; AE005176; AAK06226.1; -; Genomic_DNA.
DR PIR; H86890; H86890.
DR RefSeq; NP_268285.1; NC_002662.1.
DR RefSeq; WP_010906325.1; NC_002662.1.
DR AlphaFoldDB; Q9CDT3; -.
DR SMR; Q9CDT3; -.
DR STRING; 272623.L181494; -.
DR PaxDb; Q9CDT3; -.
DR DNASU; 1115805; -.
DR EnsemblBacteria; AAK06226; AAK06226; L181494.
DR KEGG; lla:L181494; -.
DR PATRIC; fig|272623.7.peg.2287; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_1_0_9; -.
DR OMA; QYMVGFG; -.
DR Proteomes; UP000002196; 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; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837; PTHR42837; 1.
DR Pfam; PF17820; PDZ_6; 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..428
FT /note="Putative zinc metalloprotease LL2128"
FT /id="PRO_0000088445"
FT TRANSMEM 188..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 188..282
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 428 AA; 46423 MW; 5BE5447331DE6AC8 CRC64;
MIETLITFII IFGIIVAIHE YGHLWWAKRS GILVREYAVG MGPKIFAHQA KDGTLYTIRI
LPLGGYVRLA GWGDDKTEIK KGQAASLVVS KSEVVNPEAE NSVSNIVRRI NLSEHVELEE
AIPMLITEYD FEKELFIEGE VFGEIKRYSV DHDATIIEED GTEVRIAPLD VQYQSAGVFH
KMLTNFGGPL NNFILGIIAF IVLTFVQGGV PSTTNAIGQV EKGTPAYNAG LKAGDKIEAV
NGTKTADWNN VVTEISGSKG KELKLEVSRS GKSETLSVTP KKMDGSYRVG IMQSMKTGFF
DKITGGFVQA GQSATAIFKA LGSLIARPSL DKLGGPVAIY QLSGQAARAG FPAIVYLLAM
LSINLGIVNL FPIPVLDGGK IVLNIIEAIR GKALSQEKES IITMVGVVFM LVLFVAVTWN
DILRAFVN