ID A0A1F3NXE6_9BACT Unreviewed; 987 AA.
AC A0A1F3NXE6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:OFY68915.1};
GN ORFNames=A3G23_02760 {ECO:0000313|EMBL:OFY68915.1};
OS Bacteroidetes bacterium RIFCSPLOWO2_12_FULL_37_12.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797365 {ECO:0000313|EMBL:OFY68915.1, ECO:0000313|Proteomes:UP000176497};
RN [1] {ECO:0000313|EMBL:OFY68915.1, ECO:0000313|Proteomes:UP000176497}
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, 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:OFY68915.1}.
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DR EMBL; MEPC01000042; OFY68915.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3NXE6; -.
DR STRING; 1797365.A3G23_02760; -.
DR Proteomes; UP000176497; Unassembled WGS sequence.
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:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
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; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..987
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009494639"
FT DOMAIN 73..124
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 271..438
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 603..690
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 756..894
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 987 AA; 114027 MW; EC67A695D961E84E CRC64;
MTLSSLLVFL VAFLALKPVS NLTFEPNSTE TQFMKLVEND GEFTFETVTN DPLRTRIYTL
QNGLRVYLTV YKDKPRIQTS IAVKAGSKFD PHETTGLAHY LEHMVFKGTS HFGTKDFQKE
KEELNKIEEL YEVYRTKTDP AERKKLYHQI DSISGVAASL AIAQEYDKMV GTIGAQYTNA
YTSVEQTVYV NDIPSNELER WLMIEGERFG ELVLRLFHTE LEAVYEEKNR TLDNDRRKCF
EKLFKEMFQK HTYGTQTTIG TIEHLKNPSM KKIHQYFDTY YVPNNMAMCL SGDFEPSATI
RLVNKYFGNL KPKKIPEYVP PVENPIAQPI ESNVYGYDAE SVMLGFRFPG NSNKDVLVME
MINDLLLNES AGLIDLDLNQ KQLVLEAGSF PVTMKDYSMH VLWGHPREGQ TLENLKQLLM
QEIEKIKKGD FPDWLLPAVI SDYKLRLYKK YEDNSERADA LVEAFTMDMD WKNFASKISD
LSKITKQDII RVANHYYGNN YVAVYKRTGP DTVVQKVDKP SITPVTVNRE EQSDFVKNIY
KVKPPRLKPV FLDFKQDIKE LKIHNDVSVY YKKNEENPTF SMYYYFDFGK NVDPKIEIAV
KYLEFLGTEK YSAEQFSQEL YKLGCQYNVF VSNEQMWINL SGLEENFQKA ISLFEQLLAQ
CKPDQTAFLN MIDGIIKERN DAKLSKNVIL FTAMQNYARY GGDSPFTNVL SDEQLKSLSA
EQLIFIIRSL SSLNHRILYY GTQSEKQITG NLGKHHLLPE KLFPIPVSKK FTEQDTKENK
VFWVNYKDMV QAELMFVAKS VKFDKNIVPV ASLFNEYFGE GMSSLVFQEL RESRALAYSV
SSRFRAPASA NECHYLTAYI GTQADKLNES LNGMLSLLDN MPLSENIFNM AKNSILGTME
TERITKSDIL FEYEKAKKRG LDFDLRKDIY GNVQTFTLND VKKFSDEYVK NKPRTLLVLG
SKDKINFKTL EKYGKIQELT LKDIFGY
//