ID   A8FUZ3_SHESH            Unreviewed;       611 AA.
AC   A8FUZ3;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Peptidyl-dipeptidase A {ECO:0000313|EMBL:ABV36666.1};
DE            EC=3.4.15.1 {ECO:0000313|EMBL:ABV36666.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Ssed_2057 {ECO:0000313|EMBL:ABV36666.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV36666.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV36666.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV36666.1,
RC   ECO:0000313|Proteomes:UP000002015};
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., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-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; CP000821; ABV36666.1; -; Genomic_DNA.
DR   RefSeq; WP_012142401.1; NC_009831.1.
DR   AlphaFoldDB; A8FUZ3; -.
DR   STRING; 425104.Ssed_2057; -.
DR   KEGG; sse:Ssed_2057; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_6; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000002015; 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:ABV36666.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:ABV36666.1};
KW   Protease {ECO:0000313|EMBL:ABV36666.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002015};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..611
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002720053"
SQ   SEQUENCE   611 AA;  68819 MW;  944FDC4E2DF57D9D CRC64;
     MTRLSPKLSK LSFLVALSIG ATACNSAQTS DAAAQSKTDE AKQFIQGSEK QLSELSIEIN
     RAEWIYSNFI TQDTAALSAA VGEKQTATAV KLATMAANYT QLPLDEVSLR KLNILRSSLV
     LPAPLDPKKN AELANISAEL NGLYGKGKYC FDDGRCLTQP ELSAIMAESQ NPAELLEVWK
     GWREIAKPMR PLFKREVELA NEGAKDLGYA NLSELWRSQY DMKPDEFSNE LDRLWGQVKP
     LYDSLHCYVR GELNDEYGDD VVSKDGPIPA HLLGNMWAQS WGNIYAKVAP QDADPGYDVT
     ELLAQHNYDE LKMVKQAEGF FSSLGFAELP DTFWERSLFV QPKDRDVVCH ASAWDLDDLD
     DIRIKMCIQK TAEDFTVIHH ELGHNYYQRA YKEQPFIFKN SANDGFHEAI GDTIALSITP
     SYLKQIGLLD EVPDASKDIG LLLKQALDKV AFMPFGLMID QWRWKVFSGE ITPEQYNQAW
     WDLREQYQGV KAPIARGEEN FDPGAKYHVP GNVPYTRYFL AHILQFQFHK ALCDIAGDKG
     PVHRCSIYGN REAGAKLNAM LEMGQSRPWP EALEVVTGSQ EMDARAVLDY FAPLQVWLDK
     QNSEANRQCG W
//