ID A9L194_SHEB9 Unreviewed; 621 AA.
AC A9L194;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE SubName: Full=Peptidyl-dipeptidase A {ECO:0000313|EMBL:ABX49339.1};
DE EC=3.4.15.1 {ECO:0000313|EMBL:ABX49339.1};
DE Flags: Precursor;
GN OrderedLocusNames=Sbal195_2170 {ECO:0000313|EMBL:ABX49339.1};
OS Shewanella baltica (strain OS195).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=399599 {ECO:0000313|EMBL:ABX49339.1, ECO:0000313|Proteomes:UP000000770};
RN [1] {ECO:0000313|EMBL:ABX49339.1, ECO:0000313|Proteomes:UP000000770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS195 {ECO:0000313|EMBL:ABX49339.1,
RC ECO:0000313|Proteomes:UP000000770};
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS195.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000891; ABX49339.1; -; Genomic_DNA.
DR RefSeq; WP_006087190.1; NC_009997.1.
DR AlphaFoldDB; A9L194; -.
DR GeneID; 11772316; -.
DR KEGG; sbn:Sbal195_2170; -.
DR HOGENOM; CLU_014364_3_0_6; -.
DR OMA; FTVIHHE; -.
DR Proteomes; UP000000770; 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:ABX49339.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000313|EMBL:ABX49339.1};
KW Protease {ECO:0000313|EMBL:ABX49339.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
SQ SEQUENCE 621 AA; 69445 MW; D9A5246F4BE4EDD3 CRC64;
MVISLNRRSK IALTVALTLG LTACNDAQSK TDKPASTEAA VINTARDKAQ AIAFINDAEA
KMAELSIESN RAEWIYSNFI TDDTAALSAA VGEKVSAASV KFATKAAKYA NVQLDPVNAR
KLNILRSALV LPAPLDPAKN AELAQISSEL NGLYGKGKYC FADGKCMTQP ELSSLMAESR
DPATLLEAWK GWREIAKPMR PLFQREVELA NEGAKDLGYA NLSELWRSQY DMKPDDFSQE
LDRLWGQVKP LYESLHCYVR GELNKEYGDN IAPTTGPIPA HLLGNMWAQQ WGNVYDLVAP
DNADPGYDVT ELLAKNGYDE HKMVKQAEGF FTSLGFAPLP ENFWARSLFV 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 QNTVANRQCG W
//