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   03-AUG-2022, entry version 85.
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; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=29397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 7290;
RX   PubMed=7851736; DOI=10.1111/j.1574-6968.1994.tb07299.x;
RA   Klein J., Henrich B., Plapp R.;
RT   "Cloning and nucleotide sequence analysis of the Lactobacillus delbrueckii
RT   ssp. lactis DSM7290 cysteine aminopeptidase gene pepC.";
RL   FEMS Microbiol. Lett. 124:291-299(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by
CC         hydrolysis of a carboxyamide bond of beta-aminoalanine, but also
CC         shows general aminopeptidase activity. The specificity varies
CC         somewhat with source, but amino acid arylamides of Met, Leu and Ala
CC         are preferred.; EC=3.4.22.40;
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088}.
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DR   EMBL; X80643; CAA56689.1; -; Genomic_DNA.
DR   PIR; S52865; S52865.
DR   RefSeq; WP_035165147.1; NZ_JACSVI010000052.1.
DR   AlphaFoldDB; Q48543; -.
DR   SMR; Q48543; -.
DR   MEROPS; C01.086; -.
DR   OrthoDB; 1064956at2; -.
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:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00585; Peptidase_C1B; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR004134; Peptidase_C1B.
DR   PANTHER; PTHR10363; PTHR10363; 1.
DR   Pfam; PF03051; Peptidase_C1_2; 1.
DR   PIRSF; PIRSF005700; PepC; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Protease; Thiol protease.
FT   CHAIN           1..449
FT                   /note="Aminopeptidase C"
FT                   /id="PRO_0000050590"
FT   ACT_SITE        70
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT   ACT_SITE        364
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT   ACT_SITE        385
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
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