ID A0A1F5BBH8_9BACT Unreviewed; 502 AA.
AC A0A1F5BBH8;
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=A2V57_06035 {ECO:0000313|EMBL:OGD27958.1};
OS Candidatus Aminicenantes bacterium RBG_19FT_COMBO_65_30.
OC Bacteria; Candidatus Aminicenantes.
OX NCBI_TaxID=1797277 {ECO:0000313|EMBL:OGD27958.1, ECO:0000313|Proteomes:UP000177619};
RN [1] {ECO:0000313|EMBL:OGD27958.1, ECO:0000313|Proteomes:UP000177619}
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 -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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:OGD27958.1}.
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DR EMBL; MEYF01000053; OGD27958.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5BBH8; -.
DR STRING; 1797277.A2V57_06035; -.
DR Proteomes; UP000177619; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; 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; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..502
FT /note="Peptidase M16"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009517748"
FT DOMAIN 62..91
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 252..430
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT COILED 121..148
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 502 AA; 56557 MW; BE0F03FC2CB70684 CRC64;
MTITKRIKQS CLLLAFVLAL GPAVLPAQSL EEKVTAHTLK NGLTVIFAER HGAPVFSTLY
GFKVGSVDEY PGITGTAHLF EHMAFKGTPK IGTKDYGKEK VLMDKIAQVG REWSVELAKG
DQGDKEKIAR LRADLTKLEE EQKAYIVKDE IDLVYSNVGG TGLNAGTGTD QTMYMISLPA
NRFELFCLME SERIRNTVLR EFYIERSVIQ EERKQTTDAV PTRLLSEMFM GAAFIAHPYK
NPVVGWASDI NSVTLEEAQA FKNRYYTPNN CVLAIVGDIY PEKAIPLVEK YFGDIPRGED
PPVFRTVEPK QLGERRVRFE FDAEPQLMMG YHKPNFPSKE DAAANVLAYI LTRGRTSRIY
KDLIQDKQLA VSVSGLAAFP GDRYPNLFGF NAVPRFPHTV EEVEKSVLEH VEKVKIEPVS
ERELQKVKNN IDASYIRSMS SNFGIAMTLV EYQLLYGDWK LFKKYRELIA AVTAPDVMDF
AKTYLTPENR TVAYLVKKAK AS
//
