ID   A0A1Q3TII0_9SPHI        Unreviewed;       453 AA.
AC   A0A1Q3TII0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Peptidase M16 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BGO52_00010 {ECO:0000313|EMBL:OJW02011.1};
OS   Sphingobacteriales bacterium 44-61.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895838 {ECO:0000313|EMBL:OJW02011.1, ECO:0000313|Proteomes:UP000186208};
RN   [1] {ECO:0000313|EMBL:OJW02011.1, ECO:0000313|Proteomes:UP000186208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=44-61 {ECO:0000313|EMBL:OJW02011.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OJW02011.1}.
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DR   EMBL; MKTW01000008; OJW02011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3TII0; -.
DR   STRING; 1895838.BGO52_00010; -.
DR   Proteomes; UP000186208; 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}; Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..453
FT                   /note="Peptidase M16"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012569375"
FT   DOMAIN          38..160
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          195..373
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   453 AA;  51823 MW;  9AE94AFDE81CA5AD CRC64;
     MNKKLLVAAM LATSVTAFSQ PRLPDNYYWQ KLDNGLEVVV IENHKVPLAT IEIAVKNGAY
     TEGPEYSGLS HLFEHMFFKA NKDYPDQEKF IKRTEELGMI WNGTTGDERV NYFFTFDKDS
     LNAGLKFMNA AIRFPIYRTE DMQKERPVVD GEFQRAESDP YFQLWITVGK KVWGDLFTRK
     NPIGDHDIIN SATPEKMMVI KDKYYFPNNS LLVITGDVKP AEAFAKVKAI FGDWASSGFN
     PHEKYPIPEF KPIEKTEYFV KESSIAQTPY VMYVWQGPDT RRDSVGTLAA DVFSTILGLN
     SSKWQQALVD KGLASYAGVS YQSAAHVGPV QILAVPNPGK LKEFTAEVLN QVNHFADADY
     FTDEQFQTAK DILRRNFIRA NEKPSALSST LTFWWCSASL DYYTDYMKNL MNVTRADIQN
     YLKKYIIDKP YIAGMIINED MSKQLKVNEF FKN
//