ID A0A1F5SWA6_9BACT Unreviewed; 424 AA.
AC A0A1F5SWA6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Peptidase M16 {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2478_00415 {ECO:0000313|EMBL:OGF30899.1};
OS Candidatus Falkowbacteria bacterium RIFOXYC2_FULL_36_12.
OC Bacteria; Candidatus Falkowbacteria.
OX NCBI_TaxID=1798002 {ECO:0000313|EMBL:OGF30899.1, ECO:0000313|Proteomes:UP000179001};
RN [1] {ECO:0000313|EMBL:OGF30899.1, ECO:0000313|Proteomes:UP000179001}
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:OGF30899.1}.
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DR EMBL; MFGJ01000008; OGF30899.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5SWA6; -.
DR STRING; 1798002.A2478_00415; -.
DR Proteomes; UP000179001; 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 18..161
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 167..344
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 424 AA; 48563 MW; 03A0C48B5ACD7364 CRC64;
MIEKKQFENG LRLVTIPDLS VRSVTIFVLF AVGSRYEDKD INGASHFVEH LMFKGTKKRP
NSLDISKALD SFGAEYNAAT SKDWTGYYIK IDSRHLEEAL DILSDMIYNS KFDAGEINKE
RGVILEEINM YQDNPLMYIE DILEQVVFKG STLGSEIAGP KKVIREISRK KLFDYKNTHY
VPEKTVIGIA GKIDNSIERL VKKYFQTTDK KIKGVKQVGY KDFVFDQKET RIKIIYKKTE
QVQVALGFPA YGYFDPRVYA LNLLSVILGG NMSSRLFISV REKRGLAYFV RCYPNIYQDT
GCLVIQSGLD KHRVGLAIET IVNELRRIKS TGVTVDELKK AKEYLRGKVV LALEDTASQA
DWYAKQELLQ NQILTPEQKF KKFDLVTVAD IKKVAKEIFV KEKTSLALIG PFKDEKYFEK
LLNL
//
