ID A0A1F6MDG1_9BACT Unreviewed; 419 AA.
AC A0A1F6MDG1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Peptidase M16 {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3C90_03575 {ECO:0000313|EMBL:OGH69692.1};
OS Candidatus Magasanikbacteria bacterium RIFCSPHIGHO2_02_FULL_51_14.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1798683 {ECO:0000313|EMBL:OGH69692.1, ECO:0000313|Proteomes:UP000177457};
RN [1] {ECO:0000313|EMBL:OGH69692.1, ECO:0000313|Proteomes:UP000177457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGH69692.1}.
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DR EMBL; MFQE01000068; OGH69692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6MDG1; -.
DR STRING; 1798683.A3C90_03575; -.
DR Proteomes; UP000177457; Unassembled WGS sequence.
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;
FT DOMAIN 20..159
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 169..343
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 419 AA; 47867 MW; 4E705B706B505BBA CRC64;
MFEHYQLGNR ANVYLVPQID TKSVTALVMY PVGSRYETEK MRGVSHYIEH LMFKGTKKRP
TTLALTREID RLGAEYNAFT GKEYTGYFIK VDATYTETAI DILSDMLFHS LFDAKEMEKE
KTVIVEEIRM YKDNPIMRIE DLFEESLFAG SRMGWNIAGT EDHVLSYGRD DVLAYRHRYY
QPGNATIIIA GAIDDDIRKL LARYFGKERN VHAAPKTFTP HGFGSSEKTD RIVVERKHTD
QAQLMIGFPA FRHTDKRNTA GAVMNMILGG SMSSRLFIQI RERRGLAYMV KSGGETFRDA
GFFYVRAGLD AKNINGALAV MHNEIEKIKD AGVTQRELKD AKTHIRGSLT LSLEDSSAQA
DWYARQALFM DSIKTPEQKL REIERVTNEQ IRDVARRVFH SDEMRVAVVG DVEAESVFF
//
