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Database: UniProt
Entry: D8P8G2_9BACT
LinkDB: D8P8G2_9BACT
Original site: D8P8G2_9BACT 
ID   D8P8G2_9BACT            Unreviewed;       417 AA.
AC   D8P8G2;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Putative Zn-dependent peptidase, M16 family {ECO:0000313|EMBL:CBK43794.1};
DE            EC=3.4.24.- {ECO:0000313|EMBL:CBK43794.1};
GN   ORFNames=NIDE4126 {ECO:0000313|EMBL:CBK43794.1};
OS   Nitrospira defluvii.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Nitrospira.
OX   NCBI_TaxID=330214 {ECO:0000313|EMBL:CBK43794.1, ECO:0000313|Proteomes:UP000001660};
RN   [1] {ECO:0000313|EMBL:CBK43794.1, ECO:0000313|Proteomes:UP000001660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20624973; DOI=10.1073/pnas.1003860107;
RA   Lucker S., Wagner M., Maixner F., Pelletier E., Koch H., Vacherie B.,
RA   Rattei T., Sinninghe Damste J., Spieck E., Le Paslier D., Daims H.;
RT   "A Nitrospira metagenome illuminates the physiology and evolution of
RT   globally important nitrite-oxidizing bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 0:13479-13484(2010).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; FP929003; CBK43794.1; -; Genomic_DNA.
DR   AlphaFoldDB; D8P8G2; -.
DR   STRING; 330214.NIDE4126; -.
DR   KEGG; nde:NIDE4126; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_009902_3_3_0; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000001660; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:InterPro.
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; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 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:0000313|EMBL:CBK43794.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001660}.
FT   DOMAIN          13..158
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          167..340
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   417 AA;  46901 MW;  DC93BA16DEE3B414 CRC64;
     MYRKIVLDNR LRIVAELLPT LKSVTIGIWV NVGSRDEQPG EEGLSHFLEH MFFKGTRSRT
     ATQISREIDA LGGEMNAFTT RETTTFYVKV LDQQLEAALE LLSDLFYRSR FESKEVEKEK
     QVVLEEIRMV QDDPEDLVQE LHMKHTLGSH PLGRPILGQA PRIQALGRND LVSYVGSHYD
     PERTVVAVAG NFTWRRLEQL LARYFSDSHK GVAARPSRRP PEVKGGVLVK RKALEQVHLC
     LGLQGLSAGH KDRYAAHALN GVLGGSVSSR LFQEVREKRG LVYSIYSFLS TYSDGGMTTV
     YAGTRPKEVE RVVEVVCREL KKLRTHGIDA KDLARVKNQM KGSLMLSLES SHSRMSKLAK
     DELTQGNHVS LEQMIAEIDR VTTDQVYRVA QTLLDQRCLS ITALGPIPTK SLRSFAS
//
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