ID   PEPC_LACHE              Reviewed;         449 AA.
AC   Q10744;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 59.
DE   RecName: Full=Aminopeptidase C;
DE            EC=3.4.22.40;
DE   AltName: Full=Bleomycin hydrolase;
GN   Name=pepC;
OS   Lactobacillus helveticus.
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=53/7, and CNRZ 32;
RX   MEDLINE=95010092; PubMed=7925424;
RX   DOI=10.1111/j.1432-1033.1994.00991.x;
RA   Vesanto E., Varmanen P., Steele J.L., Palva A.;
RT   "Characterization and expression of the Lactobacillus helveticus pepC
RT   gene encoding a general aminopeptidase.";
RL   Eur. J. Biochem. 224:991-997(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CNRZ 32;
RX   MEDLINE=94161512; PubMed=8117086;
RA   Fernandez L., Bhowmik T., Steele J.L.;
RT   "Characterization of the Lactobacillus helveticus CNRZ32 pepC gene.";
RL   Appl. Environ. Microbiol. 60:333-336(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.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
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DR   EMBL; Z30340; CAA82997.1; -; Genomic_DNA.
DR   EMBL; L26223; AAA25250.1; -; Genomic_DNA.
DR   PIR; S48200; S48200.
DR   HSSP; Q13867; 2CB5.
DR   MEROPS; C01.086; -.
DR   BRENDA; 3.4.22.40; 39238.
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; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Protease; Thiol protease.
FT   CHAIN         1    449       Aminopeptidase C.
FT                                /FTId=PRO_0000050591.
FT   ACT_SITE     70     70       By similarity.
FT   ACT_SITE    364    364       By similarity.
FT   ACT_SITE    385    385       By similarity.
FT   VARIANT       7      7       N -> T.
FT   VARIANT      63     63       D -> N.
FT   VARIANT     179    179       L -> V.
FT   VARIANT     234    234       N -> D.
FT   VARIANT     310    311       NN -> KS.
FT   VARIANT     333    333       A -> D.
FT   CONFLICT    373    374       IV -> NG (in Ref. 2; AAA25250).
FT   CONFLICT    435    449       QLLPWDPMGALAFKY -> NYCHGIQWVL (in Ref.
FT                                2).
SQ   SEQUENCE   449 AA;  51400 MW;  B0E5C687691B96A3 CRC64;
     MAKEINNDTI AKFENDLNNH PVFNVASHAA QENGIYKASQ NLQTKIDLDP IFSIEIDTGK
     PADQKQSGRC WMFSALNTMR HPLQKKFKLQ DFELSQNYTN FWDKFEKSNW FFENVIATAD
     KDLGDRKVSF LFATPQQDGG QWDMLCGIIE KYGIVPKSVY PETANATNSS ALNDTLNTLL
     RKDGLELRRL VNAGKSEDEV QARKEEMLND VFRVLAISTC VPPKKFNFEY RDDNHNYHID
     KDITPKEFFD KYVGMDLANH ISTINAPTSD KPFHKVFSVE YLGNVEGGRQ VRHLNLKVDE
     MKDLIIKQLN NGEVVWFGSN VVKDSERRAG LLATNLYRRD QLFDVDFSMS KADKLDSGES
     MMDHAMVITG VDIVDGKPTK WKIENSWGEK PGFKGYFVMS DSWFDSFVYQ AVINKDILPE
     DLKKAYDEGK DNPIQLLPWD PMGALAFKY
//