ID   A0A1W9QS62_9BACT        Unreviewed;       412 AA.
AC   A0A1W9QS62;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Peptidase M16 {ECO:0000313|EMBL:OQX75165.1};
GN   ORFNames=B6D61_10970 {ECO:0000313|EMBL:OQX75165.1};
OS   Bacteroidetes bacterium 4484_249.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1970778 {ECO:0000313|EMBL:OQX75165.1, ECO:0000313|Proteomes:UP000192581};
RN   [1] {ECO:0000313|Proteomes:UP000192581}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Seitz K., Teske A., Baker B.;
RT   "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT   hydrothermal sediment communities.";
RL   Submitted (MAR-2017) 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:OQX75165.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NATE01000237; OQX75165.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W9QS62; -.
DR   Proteomes; UP000192581; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 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   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          15..129
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          168..344
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   412 AA;  47191 MW;  80D8D0184A38310F CRC64;
     MIDFEKFELD NGLKVIVHKD TSTPIVAMNI LYDVGARDED PDKTGFAHLF EHLMFGGSVN
     IPKYDVPLEK AGGENNAFTN NDITNYYLTI PKQNLEIAFW LESDRMLNLA FSEKSLEVQR
     NVVIEEFKQS YLNQPYGDVW LLLRPIVYKV HPYQWSTIGK DISHIENATM EDVKAFYKKF
     YNPDNAILTV AGDIEVEEIK ELATKWFAPI EAGKKYLRTL KQEPAQNEAR NLSVERNVPF
     DSIYKVYHTY NRKNEMYHTS DLLSDLLSNG DSSRLYTKLV KEKRMFSEIN AYISGDIDNG
     MFIFTGKLIS GVKIEDAENA IIEEIEHIKN STVDDPELMK VKNKIESSLE FSEMNVLNKA
     MNLSYSELLG SADLVNMEKS KYNAVTKEGI QQAANKIFKK DNCSTLYYTA SV
//