ID   A0A0Q8EN81_9GAMM        Unreviewed;       658 AA.
AC   A0A0Q8EN81;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Peptidase M20 {ECO:0000313|EMBL:KRA41873.1};
GN   ORFNames=ASD72_14915 {ECO:0000313|EMBL:KRA41873.1};
OS   Pseudoxanthomonas sp. Root630.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=1736574 {ECO:0000313|EMBL:KRA41873.1, ECO:0000313|Proteomes:UP000051081};
RN   [1] {ECO:0000313|EMBL:KRA41873.1, ECO:0000313|Proteomes:UP000051081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root630 {ECO:0000313|EMBL:KRA41873.1,
RC   ECO:0000313|Proteomes:UP000051081};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRA41873.1, ECO:0000313|Proteomes:UP000051081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root630 {ECO:0000313|EMBL:KRA41873.1,
RC   ECO:0000313|Proteomes:UP000051081};
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:KRA41873.1}.
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DR   EMBL; LMGY01000019; KRA41873.1; -; Genomic_DNA.
DR   RefSeq; WP_056881380.1; NZ_LMGY01000019.1.
DR   AlphaFoldDB; A0A0Q8EN81; -.
DR   STRING; 1736574.ASD72_14915; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000051081; 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; -; 2.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..658
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006338729"
SQ   SEQUENCE   658 AA;  73461 MW;  016E5DE349840808 CRC64;
     MKHRHLLLAL AIGAGIATLA ACKKDEPAAE TAAAPAAPKG ETADQFVARV NDEFKKMYPE
     LTAAQWLSST YINDDSQLLA AKGNERYLTQ LNSWIEQAKQ FEGQKMSPET ARAIQLLKLA
     TAMPAPKDPA KLAELTQIAT KMEGTYGAGS YCTGEGDAKK CRQLGELEDV LRSSRDYDAQ
     LDAWQGWHTI AQPMRKDYTR FVELVNEGSK EMGFADAGEM WRSGYDMTPA EIAAETDRLW
     GQVKPLYEQL HCYTRTKLQA TYGVEKGQVN GLLPAHLMGN MWQQDWGNLW DMLEPYKGAG
     SLDITGALEK QYQADYQAAL AKAGPGPGTD KLFQAEREAQ LQVAKQMTER AQDFYTSLGM
     PKLPESYWTK TQFIKPMDRD VVCHASAWDM NMTGDVRTKM CIKPNEEDFT TIYHELGHVY
     YYLAYNKLPP LFQTGAHDGF HEAIGDTMVL AMTPDYLKSI GMVGDQQQTN EALINAQMRM
     ALAKVSFMPF GLMIDRWRWG VFDGSIKPTD YNKAWWDLKA KYQGVAPATA RSEDFFDPGA
     KYHVPGNTPY TRYFLSHVLQ FQFYKGLCDA AGYKGPLYNC SFYGNKAAGQ KFWAMLEKGA
     SQPWQGTLKE LTGTDKMDAG AVLEYFAPLQ DWLKQQNEGQ TCGWPATAPV AAAAPAKP
//