ID   G0CGZ4_XANCA            Unreviewed;       672 AA.
AC   G0CGZ4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Dipeptidyl carboxypeptidase I {ECO:0000313|EMBL:AEL06238.1};
GN   ORFNames=XCR_1338 {ECO:0000313|EMBL:AEL06238.1};
OS   Xanthomonas campestris pv. raphani 756C.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=990315 {ECO:0000313|EMBL:AEL06238.1, ECO:0000313|Proteomes:UP000001633};
RN   [1] {ECO:0000313|EMBL:AEL06238.1, ECO:0000313|Proteomes:UP000001633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=756C {ECO:0000313|EMBL:AEL06238.1,
RC   ECO:0000313|Proteomes:UP000001633};
RX   PubMed=21784931; DOI=10.1128/JB.05262-11;
RA   Bogdanove A.J., Koebnik R., Lu H., Furutani A., Angiuoli S.V., Patil P.B.,
RA   Van Sluys M.A., Ryan R.P., Meyer D.F., Han S.W., Aparna G., Rajaram M.,
RA   Delcher A.L., Phillippy A.M., Puiu D., Schatz M.C., Shumway M.,
RA   Sommer D.D., Trapnell C., Benahmed F., Dimitrov G., Madupu R., Radune D.,
RA   Sullivan S., Jha G., Ishihara H., Lee S.W., Pandey A., Sharma V.,
RA   Sriariyanun M., Szurek B., Vera-Cruz C.M., Dorman K.S., Ronald P.C.,
RA   Verdier V., Dow J.M., Sonti R.V., Tsuge S., Brendel V.P., Rabinowicz P.D.,
RA   Leach J.E., White F.F., Salzberg S.L.;
RT   "Two new complete genome sequences offer insight into host and tissue
RT   specificity of plant pathogenic Xanthomonas spp.";
RL   J. Bacteriol. 193:5450-5464(2011).
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DR   EMBL; CP002789; AEL06238.1; -; Genomic_DNA.
DR   RefSeq; WP_014507002.1; NC_017271.1.
DR   AlphaFoldDB; G0CGZ4; -.
DR   KEGG; xcp:XCR_1338; -.
DR   PATRIC; fig|990315.4.peg.1258; -.
DR   HOGENOM; CLU_014364_3_0_6; -.
DR   Proteomes; UP000001633; 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:AEL06238.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:AEL06238.1};
KW   Protease {ECO:0000313|EMBL:AEL06238.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..672
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003397833"
FT   REGION          22..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   672 AA;  74644 MW;  64680889826E9D4D CRC64;
     MNPRLLLLAL AVAAGTLSLS SCRQDAAPTP KPATTKTAPS ESADQFVARI SAEYKAAYPE
     MTAAQWLSST YINGDSQLLA AKANERALSQ LDRWIDQSKQ YAGTPMSADS ARALQLLKLM
     SALPAPRDPA KLAELTRIAA KMEGDYGAGS ACTGDGEQRR CRQLGELEQV LARSRDYDEQ
     LQAWQGWHAT AQPMRKDYQR FVELANDGAR GMGFADVGAM WRSGYDMPPA QLASETDRLW
     EQLKPLYTQL QCYARGKLDT QYGKDKGEVA GGMLPAHLMG NMWQQDWSNL WDLLQPYPGA
     GDLDITSALE KQYQGNLSAA LARNTGGDGG AAARFLAERD AQLRTAQQMT ERAQDFYTSL
     GMPKLPDTYW QRSQFIKPLD RDVVCHASAW DMNMGGEPNA GIGPDVRTKM CIRPTEEDFT
     TIYHELGHIY YDMAYNPLPP LFQNGANDGF HEAIGDTIVL AMTPKYLQSI SMVGEQQSGR
     EALINSQMRM ALSKVAFLPF GLMIDRWRWG VFDGSIPPER YNQAWWELKA TYQGVAPVSP
     RGEDFFDAGA KYHVPGNTPY TRYFLAHILQ FQFYKGLCDA AGHQGPLYEC SFYGNKEAGQ
     KFWSMLQRGS SQPWQTTLKE VTGKDTLDAG PMLEYFAPMQ EWLKQQNQGQ MCGWQAKGAT
     ATPPATPAPS TR
//