ID   A0A1Y4AML7_9BACT        Unreviewed;       412 AA.
AC   A0A1Y4AML7;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Peptidase M16 {ECO:0000313|EMBL:OUO23002.1};
GN   ORFNames=B5F90_03245 {ECO:0000313|EMBL:OUO23002.1};
OS   Alistipes sp. An31A.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=1965631 {ECO:0000313|EMBL:OUO23002.1, ECO:0000313|Proteomes:UP000196483};
RN   [1] {ECO:0000313|Proteomes:UP000196483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An31A {ECO:0000313|Proteomes:UP000196483};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-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:OUO23002.1}.
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DR   EMBL; NFIO01000002; OUO23002.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4AML7; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000196483; 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   Reference proteome {ECO:0000313|Proteomes:UP000196483};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          15..129
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          169..344
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          216..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   412 AA;  47275 MW;  710BADE3477E7215 CRC64;
     MIAYRTKRLA NGLTVVVNRD RQSKLAAVNI LYRVGARNER PDRTGFAHLF EHLMFRGTRR
     IPNFDLPVQM AAGDNNAFTN NDYTDFYITL PKDNIETALW LESDRMEGLD ITSEKLETEK
     RVVIEEFRQR YLNQPYGDQQ MLLRALAYKV HPYRWSTIGL TPDHIAAASL DEVRRFYRDH
     YHPGNAILSL SADIDEERML DLAERYFGQI APRTVTEEPI AQEPPQREAR REEVERDVPA
     TAISIAYHMG DRLSPDFYTA DLVSDLLAGG DSGRLYNRLV KERRLLASVN AYITGDRDPG
     LFVFTGQLLP ETTPEQAEEA LLGEMEELCR TPACEYETEK VKNKFEANTL FGELNVMNKA
     MNLGFYEMLG DLALINAEVD RYRSVTADDI IDFSRRTFRA ENSSTLIYKA RS
//