ID   Q082T2_SHEFN            Unreviewed;       613 AA.
AC   Q082T2;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Peptidyl-dipeptidase A {ECO:0000313|EMBL:ABI71733.1};
DE            EC=3.4.15.1 {ECO:0000313|EMBL:ABI71733.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Sfri_1887 {ECO:0000313|EMBL:ABI71733.1};
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167 {ECO:0000313|EMBL:ABI71733.1, ECO:0000313|Proteomes:UP000000684};
RN   [1] {ECO:0000313|EMBL:ABI71733.1, ECO:0000313|Proteomes:UP000000684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400 {ECO:0000313|EMBL:ABI71733.1,
RC   ECO:0000313|Proteomes:UP000000684};
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   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000447; ABI71733.1; -; Genomic_DNA.
DR   RefSeq; WP_011637349.1; NC_008345.1.
DR   AlphaFoldDB; Q082T2; -.
DR   SMR; Q082T2; -.
DR   STRING; 318167.Sfri_1887; -.
DR   KEGG; sfr:Sfri_1887; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_6; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000000684; 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:ABI71733.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:ABI71733.1};
KW   Protease {ECO:0000313|EMBL:ABI71733.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000684};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
SQ   SEQUENCE   613 AA;  68580 MW;  156109D00D453066 CRC64;
     MNLPLKRPSQ IALIVSIALG LSACNDTQEP APAPVEKIDA TAAINFINQA EADLADLSIE
     ANRAEWIYSN FITDDTAALS AAMGEKVTST SVRYATEAAK YANVELDAVN ARKLNSLRSS
     LVLPAPLDPA KNAELASIAS ELNGLYGKGK YCFADGRCLT QPELSNLMAE SKDPAVLLEA
     WQGWREIAKP MRPLFEREVE LANQGAQDLG YADLSELWRS QYDMEPEAFS AELDRLWAQI
     KPLYDSLHCY VRGELNQQYG DDVAPKTGPI PAHLLGNMWA QQWGTIYNNV APKDADPGYN
     VTELLAKNGY DEIKMVKQAE GFFTSLGFGE LPESFWTRSM FVQPQDRDVV CHASAWDLDN
     LDDIRIKMCI QKNAEDFTVI HHELGHNFYQ RAYKNQPFIF KNSANDGFHE AIGDTIALSI
     TPKYLQKIGL LETVPDASKD IGLLLKQALD KIAFMPFGLM IDQWRWQVFN GTIKPDQYNQ
     AWWDLREKYQ GVKAPIERTE ADFDPGAKYH VPGNVPYTRY FLAHVLQFQF HKALCDIAGD
     TGPVHRCSIY GNKEAGAKLN EMLEMGASKP WPEALSVVTG SDKMDAKAVL DYFAPLQVWL
     DEQNTQANRQ CGW
//