ID   U1Z9W6_9PSED            Unreviewed;       271 AA.
AC   U1Z9W6;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Peptidase M16 {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=N878_25865 {ECO:0000313|EMBL:ERI50419.1};
OS   Pseudomonas sp. EGD-AK9.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1386078 {ECO:0000313|EMBL:ERI50419.1, ECO:0000313|Proteomes:UP000016488};
RN   [1] {ECO:0000313|EMBL:ERI50419.1, ECO:0000313|Proteomes:UP000016488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EGD-Ak9 {ECO:0000313|Proteomes:UP000016488};
RA   Kapley A., Sagarkar S., Bhardwaj P., Qureshi A., Khardenavis A.,
RA   Purohit H.J.;
RT   "Indian agricultural soil isolates capable of pesticide degradation.";
RL   Submitted (AUG-2013) 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:ERI50419.1}.
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DR   EMBL; AVOF01000613; ERI50419.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1Z9W6; -.
DR   MEROPS; M16.019; -.
DR   Proteomes; UP000016488; 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; 1.
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; 1.
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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..271
FT                   /note="Peptidase M16"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004622515"
FT   DOMAIN          40..180
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          196..265
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   NON_TER         271
FT                   /evidence="ECO:0000313|EMBL:ERI50419.1"
SQ   SEQUENCE   271 AA;  30103 MW;  06835A91A397815D CRC64;
     MNAIARRSLG LLFGALCVPL TALAAALQPT HEFSLDNGLK VIVREDHRAP VVVSQLWYKV
     GSSYETAGST GLSHALEHMM FKGSRKLGPG EASRILRELG AEENAFTSDD YTAYYQVLAR
     DRLGVALELE ADRLASLQLP AAEFAKEIEV IKEERRLRTD DRPSSLAFER FKAMAYPASG
     YSIPTIGWMA DLERMQIDEL RAWYRQWYAP NNATLVVVGD VSAAEVKILA ERYFGAIERR
     AVPSAKLPLE LPAAGERRTT LHLKTQLPSL L
//