ID A0A1F8GS19_9BACT Unreviewed; 431 AA.
AC A0A1F8GS19;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Peptidase M16 {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3A33_02520 {ECO:0000313|EMBL:OGN28205.1};
OS Candidatus Yanofskybacteria bacterium RIFCSPLOWO2_01_FULL_49_25.
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1802701 {ECO:0000313|EMBL:OGN28205.1, ECO:0000313|Proteomes:UP000179047};
RN [1] {ECO:0000313|EMBL:OGN28205.1, 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:OGN28205.1}.
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DR EMBL; MGKP01000023; OGN28205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8GS19; -.
DR STRING; 1802701.A3A33_02520; -.
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 25..166
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 173..347
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 431 AA; 48655 MW; 806370FA70C4B031 CRC64;
MTTKHKHYDL HTYQNSLRLI TVPMQSTETV TVLVLVATGS RYETKDINGI SHFLEHMMFK
GTEKRPGALD ISEELDAIGA EYNAFTGQEY TGYYVKCAAE KLDVALDVIS DIFQHSKLDP
AEIDKERGAI KEEINMYYDN PARYCGTLYE ALMFGDQPLG WDIAGPKENI DRMTRDQFVD
YFQTHYFAKN TIVSVAGNIE AKGVQEKVEK YFNHIREHDA IRPAVAMESQ KAPAFKIFHK
ATDQTNINIG FRIPYGRIDD RFDALEVMSV ILGGGMSSRL FVEVREKRGL AYRISAGTSA
YDETGDFTTS AGITNTKITD ALKIILEQYA ELRDKPVPAK ELLKAKDYIK GKFLIGLEPS
DSQASYYADQ ELLEKRIQTP EEKIAKIEAI TAEDISRIAD DLFCPERLNL ALVGPFKEDD
TAIADILTSW K
//
