ID   A0A0Q4LNN3_9SPHN        Unreviewed;       603 AA.
AC   A0A0Q4LNN3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Peptidyl-dipeptidase {ECO:0000313|EMBL:KQN40904.1};
GN   ORFNames=ASE97_00380 {ECO:0000313|EMBL:KQN40904.1};
OS   Sphingomonas sp. Leaf42.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736219 {ECO:0000313|EMBL:KQN40904.1, ECO:0000313|Proteomes:UP000051880};
RN   [1] {ECO:0000313|EMBL:KQN40904.1, ECO:0000313|Proteomes:UP000051880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf42 {ECO:0000313|EMBL:KQN40904.1,
RC   ECO:0000313|Proteomes:UP000051880};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN40904.1, ECO:0000313|Proteomes:UP000051880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf42 {ECO:0000313|EMBL:KQN40904.1,
RC   ECO:0000313|Proteomes:UP000051880};
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   -!- 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:KQN40904.1}.
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DR   EMBL; LMLF01000001; KQN40904.1; -; Genomic_DNA.
DR   RefSeq; WP_055757129.1; NZ_LMLF01000001.1.
DR   AlphaFoldDB; A0A0Q4LNN3; -.
DR   PATRIC; fig|1736219.3.peg.69; -.
DR   Proteomes; UP000051880; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd06461; M2_ACE; 1.
DR   Gene3D; 1.10.1370.30; -; 1.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   PANTHER; PTHR10514:SF27; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   Pfam; PF01401; Peptidase_M2; 1.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051880};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..603
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006226062"
SQ   SEQUENCE   603 AA;  66656 MW;  EA5D54D13E48173C CRC64;
     MRTAVSAIAL TLATPALAQQ APATPPTAAD ADRFVASTEK AMFDYSIDAQ RIAWVNATYI
     TDDTDALAAR SGAIGTEMAV KYALESARYA GIRGLSPDTA RKIGILRSAI VLPAPTTPGA
     ATELANISTK LSSAYGKGKG TLGGQPINGS DIEAAMGTTR DPAKLQEMWV SWHDNVGAPM
     RKDYQRLVTI ANAGSKELGF RDTGAMWRSG YDMPADDFAK LTDQLWKEVE PLYQSLHTYV
     RWKLNEKYGD GVQGRTGPIR ADLLGNMWAQ EWGGIYDIVA PAGSGDLGYE IGDLLKAKNY
     DPVKMVRTGE GFYSSLGFQP LPQTFWERSQ IVKPADREVI CHASAWDIDN KDDIRIKMCT
     KINSDDFVTI HHELGHNYYQ RAYKNQPYLY LNGANDGFHE AIGDFVALSI TPDYLVSIGL
     LDRAKVPGPD KDIGLLLRQA MDKVAFLPFG LLMDKWRWGV FSGEIAPGDY QKAWDALRLE
     YQGIKAPVAR DASKFDPGAK YHIPASTPYM RYFLARILQF QFYKAACDQA GWKGPLHRCS
     FYGDKQVGQR LNAMLEMGAS KPWPDALQAF TGTRAMSGKA MVEYFAPLKK WLDEQNRGKP
     TGW
//