ID   I1XI87_METNJ            Unreviewed;       453 AA.
AC   I1XI87;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Peptidase {ECO:0000313|EMBL:AFI84106.1};
GN   OrderedLocusNames=Q7A_1269 {ECO:0000313|EMBL:AFI84106.1};
OS   Methylophaga nitratireducenticrescens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Methylophaga.
OX   NCBI_TaxID=754476 {ECO:0000313|EMBL:AFI84106.1, ECO:0000313|Proteomes:UP000009144};
RN   [1] {ECO:0000313|EMBL:AFI84106.1, ECO:0000313|Proteomes:UP000009144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM1 {ECO:0000313|EMBL:AFI84106.1,
RC   ECO:0000313|Proteomes:UP000009144};
RX   PubMed=22815445; DOI=10.1128/JB.00726-12;
RA   Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT   "Complete genome sequences of Methylophaga sp. strain JAM1 and Methylophaga
RT   sp. strain JAM7.";
RL   J. Bacteriol. 194:4126-4127(2012).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; CP003390; AFI84106.1; -; Genomic_DNA.
DR   RefSeq; WP_014706479.1; NC_017857.3.
DR   AlphaFoldDB; I1XI87; -.
DR   STRING; 754476.Q7A_1269; -.
DR   MEROPS; M16.019; -.
DR   KEGG; mej:Q7A_1269; -.
DR   PATRIC; fig|754476.3.peg.1252; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_009902_1_0_6; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000009144; Chromosome.
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          38..178
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          188..368
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          434..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   453 AA;  51198 MW;  F9C08948EDF65AE5 CRC64;
     MHTLKKLVWA LLIVPVIGFA QVSEYQLDNG LKLLVKPDNR APVVVSQVWY KVGSSYEHNG
     ITGISHILEH MMFKGTENLG PNEFSRIIAE NGGSQNAFTG RDYTAYFQTL EKERLEISFR
     LEAERMRNLI IDDAELLKER EVVAEERRMR TDDNPRSLLR ESMNAMAFMN SPYHHPVIGW
     MNDINHYDPE DLREWYQMWY APNNATVVVV GDVKPDEVYQ LAQEYFGPLK PEQLATVKPQ
     IEVAQRGKRT LELKAPAELP YLMMGWKVPV VKTAVEDWEP YALDVLAGIL DGGSSSRFSR
     ELIREQQVAA GISAYNSAFS RLDDVFTIAG TPAQGKSVDD VKQAVLNQLD KVKTEPVTEA
     ELQRVKTQVI ASSVYQLDSV FYQAMQLGML ETVGLDWRLV DSYPDKISAI TAEQVQQVAQ
     KYFIDDGLTV AELIPMPTDN TTPRPTSGDP HAR
//