ID A0A1G2SE30_9BACT Unreviewed; 423 AA.
AC A0A1G2SE30;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Peptidase M16 {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3B07_00720 {ECO:0000313|EMBL:OHA83068.1};
OS Candidatus Yonathbacteria bacterium RIFCSPLOWO2_01_FULL_43_27.
OC Bacteria; Candidatus Yonathbacteria.
OX NCBI_TaxID=1802726 {ECO:0000313|EMBL:OHA83068.1, ECO:0000313|Proteomes:UP000178817};
RN [1] {ECO:0000313|EMBL:OHA83068.1, ECO:0000313|Proteomes:UP000178817}
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:OHA83068.1}.
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DR EMBL; MHUV01000002; OHA83068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2SE30; -.
DR STRING; 1802726.A3B07_00720; -.
DR Proteomes; UP000178817; 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 21..161
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 168..341
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 423 AA; 47112 MW; 679CEE3C7D5AB8D0 CRC64;
MKFQKKVLPN GLKMIVAPMA DNPTVTVLVL VSAGSDYEVK EKNGISHFLE HMCFKGTTTR
PNTSDLSIEL DALGCQYNAF TGNEYTGYYA KGKSTDFEHL LDIVSDLYLN PLLKKEEIEK
EKGVIVDEIN MYEDLPMRKV HDVWAELLYG NTPAGRSIAG TREIVRGLSR EDILKYRTAH
YVARATTVIV AGNVTPKNAF KSITKQFKGI HAGKKSSKEK TKEVQSSPNV ATLYKETDQT
HLVLGVRSFS VKDKRNFVMA VLSGVLGSGM SSRLFRKLRD EMGVGYYVRA ENSLFTDHGH
LSVSAGVAND RTEEVVRAIL AEFALLKSTL VDESELNKVK EHLVGLMYLG LESSDSIAEF
CGIQELLLGE IKTPKEKERL IRAVTAVDVR TMARKIFTDK NLNLALIGPF KDTTQFKKML
TLA
//
