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Database: UniProt
Entry: A0A0F7KGN6_9PROT
LinkDB: A0A0F7KGN6_9PROT
Original site: A0A0F7KGN6_9PROT 
ID   A0A0F7KGN6_9PROT        Unreviewed;       456 AA.
AC   A0A0F7KGN6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Peptidase M16 {ECO:0000313|EMBL:AKH39630.1};
GN   ORFNames=AAW31_12550 {ECO:0000313|EMBL:AKH39630.1};
OS   Nitrosomonas communis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=44574 {ECO:0000313|EMBL:AKH39630.1, ECO:0000313|Proteomes:UP000034156};
RN   [1] {ECO:0000313|Proteomes:UP000034156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm2 {ECO:0000313|Proteomes:UP000034156};
RA   Kozlowski J.A., Kits K.D., Stein L.Y.;
RT   "Draft genome of Nitrosomonas communis strain Nm2.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AKH39630.1, ECO:0000313|Proteomes:UP000034156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm2 {ECO:0000313|EMBL:AKH39630.1,
RC   ECO:0000313|Proteomes:UP000034156};
RX   PubMed=26769932;
RA   Kozlowski J.A., Kits K.D., Stein L.Y.;
RT   "Genome Sequence of Nitrosomonas communis Strain Nm2, a Mesophilic Ammonia-
RT   Oxidizing Bacterium Isolated from Mediterranean Soil.";
RL   Genome Announc. 4:0-0(2016).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; CP011451; AKH39630.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F7KGN6; -.
DR   KEGG; nco:AAW31_12550; -.
DR   PATRIC; fig|44574.3.peg.3045; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000034156; 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   Reference proteome {ECO:0000313|Proteomes:UP000034156};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          33..179
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          189..369
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   456 AA;  51400 MW;  E8F98430E65C5D79 CRC64;
     MSVKISGLML GLPLLAIAGQ FEVSEFKLDN GLKVLVKEDH RAPVVVSQVW YRIGSSYEHD
     GITGISHMLE HMMFKGTEHH PAGEFSRIIA ANGGSENAFT GEDFTAYFQS LEKSRLEVSF
     KLEADRMRYL KLDEVEFAKE REVVLEERRL RTEDQPRDKT MELFMALAFS NGPYKNPVIG
     WPEDIKEYTL SDLQKWYRQW YAPNNATVVV VGDVQPEAVH DLAQKYFGVL APSRLPKLKS
     RTELDQTGLR RMIVKRPAKL PFLVMGYKVP VLKGTVKEWE PYALEVLTGI LDGGNGARLP
     SRLVRGKEIA AEANVGYNLY SRLPTLLTIE AVPAQGHDTA TLEQALREEI RQLLEKPVTS
     EELAQVKAQV VAHKVYEQDS GFYQAMELGM LETVGLSWSK AEEYVDKIKA VTPEQVQAVA
     RKYLVEDRLS IAYLDPLLIT DGTTTAETLL EDTHAR
//
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