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Database: UniProt/TrEMBL
Entry: E6WUZ7_PSEUU
LinkDB: E6WUZ7_PSEUU
Original site: E6WUZ7_PSEUU 
ID   E6WUZ7_PSEUU            Unreviewed;       668 AA.
AC   E6WUZ7;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   SubName: Full=Peptidyl-dipeptidase A {ECO:0000313|EMBL:ADV27996.1};
DE            EC=3.4.15.1 {ECO:0000313|EMBL:ADV27996.1};
GN   OrderedLocusNames=Psesu_2161 {ECO:0000313|EMBL:ADV27996.1};
OS   Pseudoxanthomonas suwonensis (strain 11-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV27996.1, ECO:0000313|Proteomes:UP000008632};
RN   [1] {ECO:0000313|EMBL:ADV27996.1, ECO:0000313|Proteomes:UP000008632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Ovchinnikova G., Siebers A.K., Allgaier M., Thelen M.P.,
RA   Hugenholtz P., Gladden J., Woyke T.;
RT   "Complete sequence of Pseudoxanthomonas suwonensis 11-1.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP002446; ADV27996.1; -; Genomic_DNA.
DR   RefSeq; WP_013535823.1; NC_014924.1.
DR   AlphaFoldDB; E6WUZ7; -.
DR   STRING; 743721.Psesu_2161; -.
DR   KEGG; psu:Psesu_2161; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_6; -.
DR   OMA; FTVIHHE; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000008632; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
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   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:ADV27996.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:ADV27996.1};
KW   Protease {ECO:0000313|EMBL:ADV27996.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008632};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..668
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003212469"
FT   REGION          645..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   668 AA;  74922 MW;  D80AC075E90A5637 CRC64;
     MNHRPLLLAI AVAAGLLSLS ACRKTPSPEQ EKPAARAENG ETADQFVARI NAEFKAAYPE
     LTSAQWLSST YINDDSQLVA AKANERALAQ LNAWIEEAKK FEGQPMSDDS RRALNLLKQA
     TAMPAPRDPE KLAELTRIAA KMEGAYGAGT YCSGEGAARK CRQLGELEDV LRSSRDYDAQ
     LDAWAGWHSI AQPMREDYVR FVELVNEGAR ELGYADTGAM WRSGYDMEPD AFSAETDRLW
     EQVRPLYEQL HCYTRDKLQQ TYGVERGVVG EGLLPAHLMG NMWQQDWGNL WDMLQPYKGV
     GDLDITAALE RQYQQLLSAA LHRRDPSPGP RERFEAEREA QLAMAKAMTE RAQDFYVSLG
     MPRLPESYWE KSQFIKPLDR DVVCHASAWD MNMGGADGKS PDVRTKMCIK PNEEDFTTIY
     HELGHIYYDL AYNPQPPLFQ NGANDGFHEA IGDTIVLAMT PKYLESIGLV QGQAQSHEAL
     INTQMRMALA KVSFLPFGLM IDRWRWGVFD GSITPDRYNQ AWWELKARYQ GVAPVQPRGE
     EFFDPGAKYH VPGNTPYTRY FLAHLLQFQF YKSLCEAAGH TGPLYECSFH GSEAAGEKFR
     AMLARGASQP WQATLKELTG SERIDGGAVL EYFAPLQEWL QQQNQGKSCG WQGQSAQAPK
     PEAPAKAG
//
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