ID   Q12MC7_SHEDO            Unreviewed;       612 AA.
AC   Q12MC7;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Peptidyl-dipeptidase A {ECO:0000313|EMBL:ABE55399.1};
DE            EC=3.4.15.1 {ECO:0000313|EMBL:ABE55399.1};
GN   OrderedLocusNames=Sden_2117 {ECO:0000313|EMBL:ABE55399.1};
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161 {ECO:0000313|EMBL:ABE55399.1, ECO:0000313|Proteomes:UP000001982};
RN   [1] {ECO:0000313|EMBL:ABE55399.1, ECO:0000313|Proteomes:UP000001982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS217 / ATCC BAA-1090 / DSM 15013
RC   {ECO:0000313|Proteomes:UP000001982};
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   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000302; ABE55399.1; -; Genomic_DNA.
DR   RefSeq; WP_011496554.1; NC_007954.1.
DR   AlphaFoldDB; Q12MC7; -.
DR   STRING; 318161.Sden_2117; -.
DR   KEGG; sdn:Sden_2117; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_6; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000001982; 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:ABE55399.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:ABE55399.1};
KW   Protease {ECO:0000313|EMBL:ABE55399.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001982};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
SQ   SEQUENCE   612 AA;  68439 MW;  9AE418F9166AB40B CRC64;
     MKLPFKQPSQ IALVVSVALG LSACGQQIKP VATAPAVDAK AAAEFVNDAE VKLEALSIEA
     SRAEWIYSNF ITEDTAALSA AMGEKTTSMS VQLATQAATF AGLKLDPVVA RKLNSLRSSL
     ILPAPLDPAK NAELAKISSE LNGLYGKGKY CFASGECMTQ TELSALMAES KDPQLLLEAW
     QGWRQIAKPM RSLFQREVEL ANEGARDLGF ADLSELWRSQ YDMKPQEFSN ELDRLWGEIK
     PLYDSLHCYV RGELNEQYGD EVAPKTGPIP AHLLGNMWAQ HWGTIYNSVA PKDADPGFDV
     TELLAKNGYD EVKMVKQAES FFTSLGFDAL PETFWSRSLF VQPKDRDVVC HASAWDLDNQ
     DDIRIKMCIQ KTAEDFTVIH HELGHNFYQR AYKNQPYIFK GSANDGFHEA IGDTIALSIT
     PKYLQQIGLL ETVPDASKDI GLLLQQALNK IAFMPFGLMI DQWRWQVFNG QIKPEDYNKA
     WWDLREKYQG VKAPIERTEA DFDPGAKYHV PGNVPYTRYF LAHVLQFQFH KALCDIAGDT
     GPVHRCSIYG NKEAGAKLNQ MLEMGASKPW PEALEVVTGT QQMDAKAVLD YFAPLQTWLN
     EQNTQAQRQC GW
//