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
//