ID   PEPC_LACDL              Reviewed;         449 AA.
AC   Q48543;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=Aminopeptidase C;
DE            EC=3.4.22.40;
DE   AltName: Full=Bleomycin hydrolase;
GN   Name=pepC;
OS   Lactobacillus delbrueckii subsp. lactis.
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=29397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 7290;
RX   MEDLINE=95154665; PubMed=7851736; DOI=10.1016/0378-1097(94)00444-7;
RA   Klein J., Henrich B., Plapp R.;
RT   "Cloning and nucleotide sequence analysis of the Lactobacillus
RT   delbrueckii ssp. lactis DSM7290 cysteine aminopeptidase gene pepC.";
RL   FEMS Microbiol. Lett. 124:291-299(1994).
CC   -!- CATALYTIC ACTIVITY: Inactivates bleomycin B2 (a cytotoxic
CC       glycometallopeptide) by hydrolysis of a carboxyamide bond of beta-
CC       aminoalanine, but also shows general aminopeptidase activity. The
CC       specificity varies somewhat with source, but amino acid arylamides
CC       of Met, Leu and Ala are preferred.
CC   -!- SUBUNIT: Homohexamer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
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DR   EMBL; X80643; CAA56689.1; -; Genomic_DNA.
DR   PIR; S52865; S52865.
DR   HSSP; Q13867; 2CB5.
DR   MEROPS; C01.086; -.
DR   BRENDA; 3.4.22.40; 270587.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR004134; Peptidase_C1B.
DR   PANTHER; PTHR10363; Peptidase_C1B; 1.
DR   Pfam; PF03051; Peptidase_C1_2; 1.
DR   PIRSF; PIRSF005700; PepC; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; FALSE_NEG.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; FALSE_NEG.
PE   3: Inferred from homology;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Protease; Thiol protease.
FT   CHAIN         1    449       Aminopeptidase C.
FT                                /FTId=PRO_0000050590.
FT   ACT_SITE     70     70       By similarity.
FT   ACT_SITE    364    364       By similarity.
FT   ACT_SITE    385    385       By similarity.
SQ   SEQUENCE   449 AA;  50903 MW;  6E825BBAD53CE0D8 CRC64;
     MSKEISFDTI EDFTSNLSKH PAYGVAANAA QTNGIFKASQ STQSKVDLDP TFSVEIDTGS
     VTNQKQSGRC WMFSALNTMR HSIQKEFKLK GFELSQSYTF FWDKFEKSNF FFENVIGSAD
     KPLGDRKVSF LFATPQSDGG QWDMLCGLIE KYGIVPKKVY PETANSENSR ALNDTLNTML
     RKGGLELRAL VNEGKSTEEV EAHKAELLDA IFRMLATSLG LPPKSFNFEY TDDDGNYHID
     KDITPQDFFK KYVGWDLENY ISVINGPTAD KPYNKVFSVE YLGNVVGGRQ VRHLNLELSK
     FKELIINQLK QGEVVWFGSD VSKGGDREAG LLDTKIYQRD QLFDYDFSMS KADRLDSGES
     MMNHAMVITA VDLVDDKPTK WKIENSWGDK SGFKGYFVMS DEWFDQFVYQ AVLNKAFLPE
     DVKKAYDEGK ENPIELLPWD PMGALAFDF
//