ID   B0T386_CAUSK            Unreviewed;       609 AA.
AC   B0T386;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Peptidyl-dipeptidase A {ECO:0000313|EMBL:ABZ69321.1};
DE            EC=3.4.15.1 {ECO:0000313|EMBL:ABZ69321.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Caul_0184 {ECO:0000313|EMBL:ABZ69321.1};
OS   Caulobacter sp. (strain K31).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=366602 {ECO:0000313|EMBL:ABZ69321.1};
RN   [1] {ECO:0000313|EMBL:ABZ69321.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K31 {ECO:0000313|EMBL:ABZ69321.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Stephens C., Richardson P.;
RT   "Complete sequence of chromosome of Caulobacter sp. K31.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000927; ABZ69321.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0T386; -.
DR   STRING; 366602.Caul_0184; -.
DR   KEGG; cak:Caul_0184; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_5; -.
DR   OrthoDB; 5241329at2; -.
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; -; 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.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:ABZ69321.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:ABZ69321.1};
KW   Protease {ECO:0000313|EMBL:ABZ69321.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..609
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002755850"
SQ   SEQUENCE   609 AA;  67537 MW;  435B37BDE19EEF63 CRC64;
     MKTRWLAACA AVALCAGVLP TPAARAQTTA AAATPSADQA KAFVDGAEKD LMAMGEYAAR
     MAWVQATYIT DDTNWLNAKI DAESNALSVK YAKEAARFDK TDVDPVTRRK LKLLKAALVL
     PASSRPGAAQ ELADVQSRLR ALYSTGKVTI DGETLTLDDL DDRLRTERDP AKIKAMWEAW
     HAVAKPMAGD YPKLVQLANE GSVELGYKDT GALWRSWYDM EPDAFATKTD QLWAQVAPFY
     RNLHCYVRGR LNAKYGDAVQ PKTGPIRADL TGNMWAQSWG NIYDIAAPEG LAGPGYDLTQ
     SLVAKGYDAT KMMKTGEGFY TSLGMAPLPE TFWTRSMIVR PRDREVVCHA SAWDVDNDQD
     LRVKMCTRVN ADDFYTVHHE LGHNFYQRAY AGQPYLFRGG ANDGFHEAIG DFVGLSALTP
     TYLKQIGVID TAPGAEADIP YLLDMAMDKI AFLPFGLLVD KWRWQVFSGQ VDPAHYNEAW
     WKLRTQYQGV APPGPRPADA FDPGAKFHVA DSTPYTRYFL AQVYQFQFYR AACRQAGWKG
     PLNRCSVYGD KAVGETFEKM LAMGQSKPWP EALEAFTGEK DLDASAIADY FAPLNTWLIK
     QNKGQSCGW
//