ID   A0A0Q4C2H0_9SPHN        Unreviewed;       948 AA.
AC   A0A0Q4C2H0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KQM19353.1};
GN   ORFNames=ASE49_03670 {ECO:0000313|EMBL:KQM19353.1};
OS   Novosphingobium sp. Leaf2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1735670 {ECO:0000313|EMBL:KQM19353.1, ECO:0000313|Proteomes:UP000050893};
RN   [1] {ECO:0000313|EMBL:KQM19353.1, ECO:0000313|Proteomes:UP000050893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf2 {ECO:0000313|EMBL:KQM19353.1,
RC   ECO:0000313|Proteomes:UP000050893};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQM19353.1, ECO:0000313|Proteomes:UP000050893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf2 {ECO:0000313|EMBL:KQM19353.1,
RC   ECO:0000313|Proteomes:UP000050893};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQM19353.1}.
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DR   EMBL; LMJY01000012; KQM19353.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q4C2H0; -.
DR   STRING; 1735670.ASE49_03670; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000050893; 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; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 3.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050893};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..948
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006213181"
FT   DOMAIN          61..185
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          219..311
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          712..873
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          260..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   948 AA;  103474 MW;  8DCEDBDE50535F5B CRC64;
     MRGYPIALFL AMTAMPLAAK DSTRTPPPRN DTSWAFERSD LPVDTAFRFG RLPNGMRYII
     RRNATPAGTG MVRLDVDAGS LNERSAEQGY AHFIEHMAFN GSARVPEGQM VALLEREGLA
     FGADTNASTG FDRTLYKLDL PRNETALLDT ALMLMRETAS NLTIAPQAVA RERGVVLAEM
     RDRNSWALRN AIDATGFFYP GALYAQRFPI GTTATLDAAT AASLRAFYAR EYVPANVTLV
     VVGDFDPAAV EAAIVRHFND WQAPPPPPQP DAGPVNPKDR NRAEIYLDPA LSERITVQRN
     GKWMDEPDSV AQRREALRRS VGYAIVNRRL QRIARSAEPP FRGAGFGTGD VFETARSTRL
     IIDAIDGKWR MAMDAAGSTY RRALAEGFTA AEVAEQVAQL RTAITNAAAS AGTRSNAALT
     HLALSLVDDR MVPTTPRSAL ERFEAVAPQI TPNAVMAAMK REAIKLDKPL IRFEGRKAPE
     GGAPALQTAW RAVVHAPLTA EGQSATTAFA YTDFGAPGRV VSDVRRSDFG IREIRFANGL
     MLNLKKTDLE QDRVRVSLAI DGGDMLDTRA NPHAVQMVPN LDDGGLGKHS RDDLDTILAG
     RSVSLGLRSG EETFDARAAT TPRDLEIQLQ LLAALISDPG YRPEGEVRYR QAINNYFAQL
     DATPASALQA RLGGILSDED PRFSLGKLED YRQLTYAGLK RDIGDRLVHG AIEISIVGDI
     DEDATIALVA RTFGALPARE AAFRDHPEQP PRVFTADRRP RVIRHSGPAD QALLRIVWPT
     RDDADATEAL RLELLQEVTG IELTDQLRET LGKAYSPGAA SYLSHAWKGY GYFLVNASVD
     VAQVPATRAA IREVVTDLRA APVSADILLR ARQPMIERLQ NALKGNGGWM NLTARAQSQP
     DRIARFANAR AQLLAMTAAD VQQAARRYLA PDAGLEVLVL AKDVPEPR
//