ID M5J4C7_9LACO Unreviewed; 425 AA.
AC M5J4C7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:EKW99058.1};
GN ORFNames=D271_04644 {ECO:0000313|EMBL:EKW99058.1};
OS Ligilactobacillus saerimneri 30a.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1227363 {ECO:0000313|EMBL:EKW99058.1, ECO:0000313|Proteomes:UP000011912};
RN [1] {ECO:0000313|EMBL:EKW99058.1, ECO:0000313|Proteomes:UP000011912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30a {ECO:0000313|EMBL:EKW99058.1,
RC ECO:0000313|Proteomes:UP000011912};
RX PubMed=23405290;
RA Romano A., Trip H., Campbell-Sills H., Bouchez O., Sherman D.,
RA Lolkema J.S., Lucas P.M.;
RT "Genome Sequence of Lactobacillus saerimneri 30a (Formerly Lactobacillus
RT sp. Strain 30a), a Reference Lactic Acid Bacterium Strain Producing
RT Biogenic Amines.";
RL Genome Announc. 1:E00097-E00012(2013).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKW99058.1}.
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DR EMBL; ANAG01000013; EKW99058.1; -; Genomic_DNA.
DR RefSeq; WP_009553843.1; NZ_ANAG01000013.1.
DR AlphaFoldDB; M5J4C7; -.
DR STRING; 1227363.D271_04644; -.
DR MEROPS; M16.A20; -.
DR GeneID; 80986807; -.
DR PATRIC; fig|1227363.6.peg.911; -.
DR Proteomes; UP000011912; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000011912};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 30..172
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 181..342
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 425 AA; 47862 MW; D09FFBE1C0823FD0 CRC64;
MQETLYPLFA ERMQTERLAN GLLVNMIARP NFHKTYAILT VDFGSIDDTF TTEQGEKITV
PAGIAHFLEH KLFEKKDHDA FDLFGKYGAD ANAFTSYTRT SYLFATTSHL DECMNVLLDF
VQTPYFTEQT VAKEKGIIEQ EIKMYDDDPS WQLYQKTMAN LYPGSQLSLD IAGSASSIAQ
ITAQDLYTCY RHFYQPSNMN LFVIGNFVPD ELLAMIKQNQ AQKTFPEKVV PQRFFAPLAQ
PVVPQTVVPL AVKVPKVMLG IRGTEALPMN REGLKKKVAL ELLLHLLFAE TSPTYQELYD
QGIVDDSFDY ELQVERGFYF VLVDGNTRQP EAFVAAIKEI LQTAPTTVAH LTEELALAKK
EFLGQTIKSI NSLEAIANRY EGPLFGYATI FDLVPLVQEV TLADVLAATK IIDFDNLTIN
QVVPQ
//
