(data stored in SCRATCH zone)

HOGENOM: PSEP1_1_PE1002

ID   PSEP1_1_PE1002                       STANDARD;      PRT;   497 AA.
AC   PSEP1_1_PE1002; A5VZ69;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Probable cytosol aminopeptidase; EC=3.4.11.1;AltName:
DE   Full=Leucine aminopeptidase; Short=LAP; EC=3.4.11 10;AltName: Full=Leucyl
DE   aminopeptidase; (PSEP1_1.PE1002).
GN   Name=pepA; OrderedLocusNames=Pput_1018;
OS   PSEUDOMONAS PUTIDA F1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PSEP1_1.PE1002.
CC       Pseudomonas putida F1 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:AMPA_PSEP1
CC   -!- FUNCTION: Presumably involved in the processing and regular
CC       turnover of intracellular proteins. Catalyzes the removal of
CC       unsubstituted N-terminal amino acids from various peptides (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, Xaa-|-
CC       Yaa-, in which Xaa is preferably Leu, but may be other amino acids
CC       including Pro although not Arg or Lys, and Yaa may be Pro. Amino
CC       acid amides and methyl esters are also readily hydrolyzed, but
CC       rates on arylamides are exceedingly low.
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid,
CC       preferentially leucine, but not glutamic or aspartic acids.
CC   -!- COFACTOR: Binds 2 manganese ions per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC   -!- GENE_FAMILY: HOG000243132 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A5VZ69; -.
DR   EMBL; CP000712; ABQ77179.1; -; Genomic_DNA.
DR   RefSeq; YP_001266363.1; NC_009512.1.
DR   ProteinModelPortal; A5VZ69; -.
DR   SMR; A5VZ69; 1-496.
DR   STRING; A5VZ69; -.
DR   GeneID; 5194167; -.
DR   GenomeReviews; CP000712_GR; Pput_1018.
DR   KEGG; ppf:Pput_1018; -.
DR   eggNOG; COG0260; -.
DR   OMA; KYDWAHL; -.
DR   ProtClustDB; PRK00913; -.
DR   BioCyc; PPUT351746:PPUT_1018-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   HAMAP; MF_00181; Cytosol_peptidase_M17; 1; -.
DR   InterPro; IPR011356; Peptidase_M17.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   InterPro; IPR023042; Peptidase_M17_cytosol_amino.
DR   InterPro; IPR008283; Peptidase_M17_N.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   Pfam; PF02789; Peptidase_M17_N; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
DR   PROSITE; PS00631; CYTOSOL_AP; 1.
DR   HOGENOMDNA; PSEP1_1.PE1002; -.
KW   leucyl aminopeptidase;
KW   Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Manganese;
KW   Metal-binding; Protease.
SQ   SEQUENCE   497 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MELVVKSVAA ASVKTATLVL PVGENRKLGA VAKAVDQASE GAISAVLKRG DLAGKPGQTL
     LLQNLPGLKA ERVLLVGSGK EEALGDRAWR KLVASVAGVL KGLNGTDAVL ALDDIAVSNR
     DAHYGKYRLL AETLLDGEYV FDRFKSQKAE PRALKKVTLL ADKAGQAEVE RAVKHASAIA
     SGMAFTRDLG NLPPNLCHPS FLAEQAKELG KAHKALKVEV LDEKKIKDLG MGAFYAVGQG
     SDQPPRLIML NYQGGKKADK PFVLVGKGIT FDTGGISLKP GAGMDEMKYD MCGAASVFGT
     LRAVLELQLP INLVCLLACA ENMPSGGATR PGDIVTTMSG QTVEILNTDA EGRLVLCDTL
     TYAERFKPQA VIDIATLTGA CIVALGSHTS GLMGNNDDLV GQLLDAGKRA DDRAWQLPLF
     DEYQEQLDSP FADMGNIGGP KAGTITAGCF LSRFAKAYNW AHMDIAGTAW VSGGKDKGAT
     GRPVPLLTQY LLDRAGA
//

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