ID G0B071_9GAMM Unreviewed; 621 AA.
AC G0B071;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Peptidyl-dipeptidase A {ECO:0000313|EMBL:AEG11548.1};
DE EC=3.4.15.1 {ECO:0000313|EMBL:AEG11548.1};
GN ORFNames=Sbal175_2295 {ECO:0000313|EMBL:AEG11548.1};
OS Shewanella baltica BA175.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=693974 {ECO:0000313|EMBL:AEG11548.1, ECO:0000313|Proteomes:UP000002249};
RN [1] {ECO:0000313|EMBL:AEG11548.1, ECO:0000313|Proteomes:UP000002249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA175 {ECO:0000313|EMBL:AEG11548.1,
RC ECO:0000313|Proteomes:UP000002249};
RX PubMed=22328742; DOI=10.1128/JB.06468-11;
RA Caro-Quintero A., Auchtung J., Deng J., Brettar I., Hofle M., Tiedje J.M.,
RA Konstantinidis K.T.;
RT "Genome sequencing of five Shewanella baltica strains recovered from the
RT oxic-anoxic interface of the Baltic Sea.";
RL J. Bacteriol. 194:1236-1236(2012).
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DR EMBL; CP002767; AEG11548.1; -; Genomic_DNA.
DR RefSeq; WP_006081558.1; NC_017571.1.
DR AlphaFoldDB; G0B071; -.
DR KEGG; sbb:Sbal175_2295; -.
DR HOGENOM; CLU_014364_3_0_6; -.
DR Proteomes; UP000002249; 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:AEG11548.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000313|EMBL:AEG11548.1};
KW Protease {ECO:0000313|EMBL:AEG11548.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
SQ SEQUENCE 621 AA; 69363 MW; 7DB638D98712C9CD CRC64;
MVISLNRRSK IALTVALTLG LTACNDAQSK TDKPASTEAA VINTAPDKVQ AIAFINDAEA
KMAELSIESN RAEWIYSNFI TDDTAALSAA VGEKVSAASV KFATEAAKYA NVQLDPVNAR
KLNILRSALV LPAPLDPAKN AELAQISSEL NGLYGKGKYC FADGKCMTQP ELSSLMAESR
DPATLLEAWK GWREIAKPMR PLFQREVELA NEGAKDLGYA NLSELWRSQY DMKPDDFSQE
LDRLWGQVKP LYESLHCYVR GELNKEYGDT VAPTTGPIPA HLLGNMWAQQ WGNVYDLVAP
DNADPGYDVT ELLAKNGYDE HKMVKQAEGF FTSLGFAPLP ESFWARSLFV 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 QNTTANRQCG W
//