ID A0A1F4N2P2_9BACT Unreviewed; 448 AA.
AC A0A1F4N2P2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Peptidase M16 {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2Y94_06885 {ECO:0000313|EMBL:OGB65640.1};
OS Caldithrix sp. RBG_13_44_9.
OC Bacteria; Calditrichota; Calditrichia; Calditrichales; Calditrichaceae;
OC Caldithrix.
OX NCBI_TaxID=1797576 {ECO:0000313|EMBL:OGB65640.1, ECO:0000313|Proteomes:UP000179285};
RN [1] {ECO:0000313|EMBL:OGB65640.1, ECO:0000313|Proteomes:UP000179285}
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:OGB65640.1}.
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DR EMBL; MESS01000082; OGB65640.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4N2P2; -.
DR STRING; 1797576.A2Y94_06885; -.
DR Proteomes; UP000179285; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 35..182
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 190..367
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 448 AA; 51693 MW; F56EF5F17DC105CE CRC64;
MDYQKHTPFR FHKKLVSEPE EYQLTGFQLE NGLQVIMLKN HQVPVVAVDI WYKVGSKDEK
PGKSGFAHLF EHMMFEGSEN VGKAEHMKLL TDVGGTVNGS TTQDRTNYWQ VVPANQLELA
LWLEADRMRS LKINLENFEN QRATVKEERR LRIDNQPYMP VIYELKDQIS YRNFAYQHSV
MGSMEDLDRA TLEDVTAFHS LYYRPNNAVM AVVGDFTVQQ AYTLVKKYFS KIPTGAAIPA
VDLSESRCQR EVRFTFPDSF APFPAILISQ LIPERTHSSF YPLELLEKIL FDGESSRFYR
KLVEEEQLAL HVVGGQDGKF GPALFFLFAQ LHPEKKLLDL EKTIYAEFEQ LQSRGVSEEE
LEKAKNKVRT DFVSQQESVR SLADTLCMYH TVYQQPERFF TELERFEKIT ATEVQAAAKE
FLGPDGRSVI EIIPRKQATE ELKPDNLS
//
