ID A0A1F8GUD9_9BACT Unreviewed; 423 AA.
AC A0A1F8GUD9;
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=A3A33_02080 {ECO:0000313|EMBL:OGN28266.1};
OS Candidatus Yanofskybacteria bacterium RIFCSPLOWO2_01_FULL_49_25.
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1802701 {ECO:0000313|EMBL:OGN28266.1, ECO:0000313|Proteomes:UP000179047};
RN [1] {ECO:0000313|EMBL:OGN28266.1, ECO:0000313|Proteomes:UP000179047}
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:OGN28266.1}.
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DR EMBL; MGKP01000022; OGN28266.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8GUD9; -.
DR STRING; 1802701.A3A33_02080; -.
DR Proteomes; UP000179047; 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 11..152
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 158..342
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 423 AA; 46775 MW; 61717404EBA36712 CRC64;
MGNGLWVVHK EMPNPLVALT IHIKGGSSVE QPEEIGSAHF LEHMVFKAGE KFPSEELISG
LIEQEGAMPN AYTSHDRICF YALTQSNVEL MFDILSDCII RPLFKADDIS TELGRVLQEI
AEDDDDPKEV HARLFSRMIW GRHPYGESIT GTAEQVSSLT RDTFLNYHAK YFVPRNMVLS
VAGGIKSEKV FELAFKYFGD GFERPYGRAI LPSVDFSYVP DRKLFLREND LKQLKCTMGT
LPAEWIRSQK GFEKSRVTAT LLGVILGGGT SSRLFSKVSS QKGLVYYIQA GASVYENAGN
FRIDFGADPV NVVPAVAMIF DELDSILING ITEKELQKAK NIYKTSVATH LESALNIAFA
GGSAEMHGLD LHTSEEFFDS YVDPVTVIDI MAAAKDLLPK SKFYLAALGK VADNAKALES
MLS
//
