ID   A3D4S9_SHEB5            Unreviewed;       621 AA.
AC   A3D4S9;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=Peptidyl-dipeptidase A {ECO:0000313|EMBL:ABN61742.1};
DE            EC=3.4.15.1 {ECO:0000313|EMBL:ABN61742.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Sbal_2246 {ECO:0000313|EMBL:ABN61742.1}, Sbal_4532
GN   {ECO:0000313|EMBL:ABN63895.1};
OS   Shewanella baltica (strain OS155 / ATCC BAA-1091).
OG   Plasmid pSbal01 {ECO:0000313|EMBL:ABN63895.1,
OG   ECO:0000313|Proteomes:UP000001557}.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=325240 {ECO:0000313|EMBL:ABN61742.1, ECO:0000313|Proteomes:UP000001557};
RN   [1] {ECO:0000313|EMBL:ABN61742.1, ECO:0000313|Proteomes:UP000001557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS155 {ECO:0000313|EMBL:ABN61742.1}, and OS155 / ATCC BAA-1091
RC   {ECO:0000313|Proteomes:UP000001557};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA   Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS155.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABN63895.1, ECO:0000313|Proteomes:UP000001557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS155 {ECO:0000313|EMBL:ABN63895.1}, and OS155 / ATCC BAA-1091
RC   {ECO:0000313|Proteomes:UP000001557};
RC   PLASMID=pSbal01 {ECO:0000313|EMBL:ABN63895.1,
RC   ECO:0000313|Proteomes:UP000001557};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA   Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT   "Complete sequence of plasmid pSbal01 of Shewanella baltica OS155.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000563; ABN61742.1; -; Genomic_DNA.
DR   EMBL; CP000564; ABN63895.1; -; Genomic_DNA.
DR   RefSeq; WP_011839917.1; NC_009052.1.
DR   AlphaFoldDB; A3D4S9; -.
DR   STRING; 325240.Sbal_2246; -.
DR   KEGG; sbl:Sbal_2246; -.
DR   KEGG; sbl:Sbal_4532; -.
DR   HOGENOM; CLU_014364_3_0_6; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000001557; Chromosome.
DR   Proteomes; UP000001557; Plasmid pSbal01.
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:ABN61742.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:ABN61742.1};
KW   Plasmid {ECO:0000313|EMBL:ABN63895.1};
KW   Protease {ECO:0000313|EMBL:ABN61742.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..621
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007909426"
SQ   SEQUENCE   621 AA;  69352 MW;  DE1E393FBDB4EA08 CRC64;
     MVISLNRRSK IALTVALALG LTACNDAQSK TDKSASTEAA VINTAPDKTQ AIAFINDAEA
     KMAELSIESN RAEWIYSNFI TDDTAALSAA VGEKVSAASV KFATEAAKYA NVQLDPVNAR
     KLNILRSALV LPAPLDPAKN AELAQISSEL NGLYGKGKYC FTDGKCMTQP ELSSLMAESR
     DPATLLEAWK GWREIAKPMR PLFQREVELA NEGAKDLGYA NLSELWRSQY DMKPDDFSQE
     LDRLWGQVKP LYESLHCYVR GELNKEYGDN IAPTTGPIPA HLLGNMWAQQ WGNVYDLVAP
     DNADPGYDVT ELLAKNGYDE HKMVKQAEGF FTSLGFAPLP ESFWARSLFV QPKDRDVVCH
     ASAWDLDNID DIRIKMCIQK TAEDFSVIHH ELGHNFYQRA YKQQPFLFKN SANDGFHEAI
     GDTIALSITP SYLKQIGLLD EVPDASKDIG LLLKQALDKI AFLPFGLMID QWRWKVFSGE
     ITPAQYNQAW WDLREKYQGV KAPTKRSEAD FDPGAKYHVP GNVPYTRYFL AHILQFQFHQ
     ALCETAGDKG PVHRCSIYGN QAAGEKLNKM LELGLSKPWP EALKEVTGKE TMDAKAVLDY
     FAPLKTWLDE QNTAANRQCG W
//