ID   D2UCL9_XANAP            Unreviewed;       654 AA.
AC   D2UCL9;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Hypothetical conserved peptidyl-dipeptidase protein {ECO:0000313|EMBL:CBA15405.1};
DE            EC=3.4.15.- {ECO:0000313|EMBL:CBA15405.1};
GN   OrderedLocusNames=XALc_0887 {ECO:0000313|EMBL:CBA15405.1};
OS   Xanthomonas albilineans (strain GPE PC73 / CFBP 7063).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=380358 {ECO:0000313|EMBL:CBA15405.1, ECO:0000313|Proteomes:UP000001890};
RN   [1] {ECO:0000313|EMBL:CBA15405.1, ECO:0000313|Proteomes:UP000001890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GPE PC73 / CFBP 7063 {ECO:0000313|Proteomes:UP000001890};
RX   PubMed=20017926; DOI=10.1186/1471-2164-10-616;
RA   Pieretti I., Royer M., Barbe V., Carrere S., Koebnik R., Cociancich S.,
RA   Couloux A., Darrasse A., Gouzy J., Jacques M.A., Lauber E., Manceau C.,
RA   Mangenot S., Poussier S., Segurens B., Szurek B., Verdier V., Arlat M.,
RA   Rott P.;
RT   "The complete genome sequence of Xanthomonas albilineans provides new
RT   insights into the reductive genome evolution of the xylem-limited
RT   Xanthomonadaceae.";
RL   BMC Genomics 10:616-616(2009).
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DR   EMBL; FP565176; CBA15405.1; -; Genomic_DNA.
DR   RefSeq; WP_012915415.1; NC_013722.1.
DR   AlphaFoldDB; D2UCL9; -.
DR   STRING; 380358.XALC_0887; -.
DR   GeneID; 57876208; -.
DR   KEGG; xal:XALC_0887; -.
DR   PATRIC; fig|29447.3.peg.881; -.
DR   eggNOG; COG1164; Bacteria.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000001890; 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:CBA15405.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:CBA15405.1};
KW   Protease {ECO:0000313|EMBL:CBA15405.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001890};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..654
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003037045"
SQ   SEQUENCE   654 AA;  73960 MW;  CB3D7FCBAD8DF7FF CRC64;
     MNHRHPLLGL CIAASLLFLS ACRKDAAPEN VAPATPHAIG ESADQFVARI NEQYRKQLPE
     LTTAQWLSAT YINADTQRLA SEANARWLTT LNGWIAQAKR YQGQPMSADS ARALQRLKQM
     TAMPAPHDPA KLNELTALAA KMEGAYAVAT SCSGEGDARR CRQLDELEEV LRRSRDYDQQ
     LDAWQSWHAT AQPLRKDYPR FVELVNEGAR EMGYADTGAM WRSGYDMPPA QLVAETDRLW
     AQVKPLYEQL HCYARSKLDT EYGKDKGEVA GGLLPAHLLG NMWQQDWSNL WDLLQPYRDA
     SNLDITDALE RQYQSDLSAA LARRNGDTSA EARFMAQREA QSLSARQMNE HAQDFYTSLA
     MPKLPDSYWS RSQFIKPLDR DVDCHASAWN MDMAGDVRAK MCVKPDEEDF ATLYHELGHV
     YYYLAYDSLP PLFQSGANDG FHEAIGDTVV LALTPQYLHT IALTETPQVS REALINTQMR
     MALNKVAFLP FGLMIDRWRW GVFDGSIGPD RYNQAWWELK AKYQGVAPVA PRGEAFFDPG
     AKYHVPANTP YTRYFLSHIL QFQFYKSLCD AAGHKGPLYA CTFYGNKEAG QKFWSMLQRG
     ASQPWQATLK ELTGSERLDA GPLLEYFAPI QQWLKQQNQG RLCGWDTPKP TTAH
//