ID   A0A0Q4QQH3_9GAMM        Unreviewed;       437 AA.
AC   A0A0Q4QQH3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KQN97438.1};
GN   ORFNames=ASF01_12330 {ECO:0000313|EMBL:KQN97438.1};
OS   Stenotrophomonas sp. Leaf70.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=1736233 {ECO:0000313|EMBL:KQN97438.1, ECO:0000313|Proteomes:UP000051583};
RN   [1] {ECO:0000313|EMBL:KQN97438.1, ECO:0000313|Proteomes:UP000051583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf70 {ECO:0000313|EMBL:KQN97438.1,
RC   ECO:0000313|Proteomes:UP000051583};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN97438.1, ECO:0000313|Proteomes:UP000051583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf70 {ECO:0000313|EMBL:KQN97438.1,
RC   ECO:0000313|Proteomes:UP000051583};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:KQN97438.1}.
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DR   EMBL; LMLT01000007; KQN97438.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q4QQH3; -.
DR   Proteomes; UP000051583; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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; IPR001431; Pept_M16_Zn_BS.
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.
DR   PROSITE; PS00143; INSULINASE; 1.
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          37..182
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          190..364
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   437 AA;  48206 MW;  8BAB59274AFFDAC8 CRC64;
     MAATAASAEP VKVNGFTHVK SLDGIDEYRL DANGLSVLLL PNHAAPVVTF QVTYRVGSRN
     EVTGSTGGTH LLEHLMFMGS THFDGENNVD TYLDRVGAGF NATTSLDRTN YYATLPPAAL
     DGYIAIEADR MRGLLLREKD RQSEMTVVRN EYERNENNPN GALMKLMWAT AYSAHPYHHP
     VIGWRSDIEN VSIEKLRAFY DTFYWPNNAT VTVVGDIDSA KVLASIGEKF GKVPRSPHAI
     PEVYTTEPEQ QGERRVTLRR AGETGTVMMA YKAPAGVDKD IPALNVLELV LQGGRSARLP
     RALVDTSKAV AVSGGMYQQR DPSLFMLSVA LAPDSRHEDI EKTVRDEIAK VARDGVTVEE
     IKRVLGPYRA EEAYRRDGTD QAADALNEFI AMGDWTLYST ALKDLEKVTP ADVQRVAGKY
     FTAEQSTIGW FVPESSK
//