ID   A9L194_SHEB9            Unreviewed;       621 AA.
AC   A9L194;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Peptidyl-dipeptidase A {ECO:0000313|EMBL:ABX49339.1};
DE            EC=3.4.15.1 {ECO:0000313|EMBL:ABX49339.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Sbal195_2170 {ECO:0000313|EMBL:ABX49339.1};
OS   Shewanella baltica (strain OS195).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399599 {ECO:0000313|EMBL:ABX49339.1, ECO:0000313|Proteomes:UP000000770};
RN   [1] {ECO:0000313|EMBL:ABX49339.1, ECO:0000313|Proteomes:UP000000770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS195 {ECO:0000313|EMBL:ABX49339.1,
RC   ECO:0000313|Proteomes:UP000000770};
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA   Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS195.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000891; ABX49339.1; -; Genomic_DNA.
DR   RefSeq; WP_006087190.1; NC_009997.1.
DR   AlphaFoldDB; A9L194; -.
DR   GeneID; 11772316; -.
DR   KEGG; sbn:Sbal195_2170; -.
DR   HOGENOM; CLU_014364_3_0_6; -.
DR   Proteomes; UP000000770; 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; -; 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   Carboxypeptidase {ECO:0000313|EMBL:ABX49339.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:ABX49339.1};
KW   Protease {ECO:0000313|EMBL:ABX49339.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
SQ   SEQUENCE   621 AA;  69445 MW;  D9A5246F4BE4EDD3 CRC64;
     MVISLNRRSK IALTVALTLG LTACNDAQSK TDKPASTEAA VINTARDKAQ AIAFINDAEA
     KMAELSIESN RAEWIYSNFI TDDTAALSAA VGEKVSAASV KFATKAAKYA NVQLDPVNAR
     KLNILRSALV LPAPLDPAKN AELAQISSEL NGLYGKGKYC FADGKCMTQP ELSSLMAESR
     DPATLLEAWK GWREIAKPMR PLFQREVELA NEGAKDLGYA NLSELWRSQY DMKPDDFSQE
     LDRLWGQVKP LYESLHCYVR GELNKEYGDN IAPTTGPIPA HLLGNMWAQQ WGNVYDLVAP
     DNADPGYDVT ELLAKNGYDE HKMVKQAEGF FTSLGFAPLP ENFWARSLFV QPKDRDVVCH
     ASAWDLDNLD DIRIKMCIQK TAEDFSVIHH ELGHNFYQRA YKQQPFLFKN SANDGFHEAI
     GDTIALSITP SYLKQIGLLD EVPDASKDIG LLLKQALDKI AFLPFGLMID QWRWKVFSGE
     ITPAQYNQAW WDLREKYQGV KAPTKRSEAD FDPGAKYHVP GNVPYTRYFL AHILQFQFHQ
     ALCETAGDKG PVHRCSIYGN QAAGEKLNKM LELGLSKPWP EALKEVTGKE TMDAKAVLDY
     FAPLKTWLDE QNTVANRQCG W
//