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Database: UniProt/TrEMBL
Entry: B1KGV2_SHEWM
LinkDB: B1KGV2_SHEWM
Original site: B1KGV2_SHEWM 
ID   B1KGV2_SHEWM            Unreviewed;       612 AA.
AC   B1KGV2;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   05-JUL-2017, entry version 57.
DE   SubName: Full=Peptidyl-dipeptidase A {ECO:0000313|EMBL:ACA86821.1};
DE            EC=3.4.15.1 {ECO:0000313|EMBL:ACA86821.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Swoo_2544 {ECO:0000313|EMBL:ACA86821.1};
OS   Shewanella woodyi (strain ATCC 51908 / MS32).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=392500 {ECO:0000313|EMBL:ACA86821.1, ECO:0000313|Proteomes:UP000002168};
RN   [1] {ECO:0000313|EMBL:ACA86821.1, ECO:0000313|Proteomes:UP000002168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51908 / MS32 {ECO:0000313|Proteomes:UP000002168};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella woodyi ATCC 51908.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000961; ACA86821.1; -; Genomic_DNA.
DR   RefSeq; WP_012325162.1; NC_010506.1.
DR   ProteinModelPortal; B1KGV2; -.
DR   STRING; 392500.Swoo_2544; -.
DR   EnsemblBacteria; ACA86821; ACA86821; Swoo_2544.
DR   KEGG; swd:Swoo_2544; -.
DR   eggNOG; ENOG4105EAJ; Bacteria.
DR   eggNOG; ENOG410XPJ3; LUCA.
DR   HOGENOM; HOG000292210; -.
DR   KO; K01283; -.
DR   OMA; DFLTAHH; -.
DR   OrthoDB; POG091H0VNC; -.
DR   BioCyc; SWOO392500:GI2C-2587-MONOMER; -.
DR   Proteomes; UP000002168; 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   CDD; cd06461; M2_ACE; 1.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; PTHR10514; 1.
DR   Pfam; PF01401; Peptidase_M2; 1.
DR   PRINTS; PR00791; PEPDIPTASEA.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:ACA86821.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002168};
KW   Hydrolase {ECO:0000313|EMBL:ACA86821.1};
KW   Protease {ECO:0000313|EMBL:ACA86821.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002168};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    612       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002766592.
SQ   SEQUENCE   612 AA;  68946 MW;  3F066032D526AD2E CRC64;
     MKLSTARLSK ISLLVGLTLA ATACQKVQSD ETVSAQTSVA EAEQFITQSE QALSELSIEV
     NRSEWIYSNF ITEDTAALSA SVGEKYTATT VKLATVAANY TQLPLSADNL RKLNILRSAL
     VLPAPLDPKK NAELASISSE LNGLYGKGKY CFDDGRCLTQ PELSAIMGES QDPALLLEVW
     KGWRDIAKPM RPLFKREVEL ANEGARDLGY ADLSELWRSQ YDMEPDEFSN ELDRLWGQVK
     PLYDSLHCYV RGELNEKYGD DVVSKQGPIP AHLLGNMWAQ SWGNIYNQVA PEDADPGYDV
     TELLAQHGYD EIKMVKQAES FFSSLGFEPL PDTFWERSLF VQPKDRDVVC HASAWALDDK
     DDIRIKMCIQ KTAEDFTVIH HELGHNYYQR AYKNQPFIFK NSANDGFHEA IGDTVALSIT
     PNYLKQIGLL DEVPDASKDI GLLLKQALDK VAFMPFGLMI DQWRWKVFSG EITPEQYNQA
     WWELREKYQG VKSPISRDEK DFDPGAKYHV PGNVPYTRYF LAHILQFQFH KALCDIAGDK
     GPVHRCSIYG NKDAGTKLNT MLEMGQSQPW PEALAVVTGS KEMDANAVLD YFAPLQTWLN
     EQNSQANRQC GW
//
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