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   03-AUG-2022, entry version 89.
DE   RecName: Full=Aminopeptidase C;
DE            EC=3.4.22.40;
DE   AltName: Full=Bleomycin hydrolase;
GN   Name=pepC;
OS   Lactobacillus helveticus (Lactobacillus suntoryeus).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=53/7, and CNRZ 32;
RX   PubMed=7925424; 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 gene
RT   encoding a general aminopeptidase.";
RL   Eur. J. Biochem. 224:991-997(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CNRZ 32;
RX   PubMed=8117086; DOI=10.1128/aem.60.1.333-336.1994;
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:
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.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
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DR   EMBL; Z30340; CAA82997.1; -; Genomic_DNA.
DR   EMBL; L26223; AAA25250.1; -; Genomic_DNA.
DR   PIR; S48200; S48200.
DR   AlphaFoldDB; Q10744; -.
DR   SMR; Q10744; -.
DR   MEROPS; C01.086; -.
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; IPR025660; Pept_his_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.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Protease; Thiol protease.
FT   CHAIN           1..449
FT                   /note="Aminopeptidase C"
FT                   /id="PRO_0000050591"
FT   ACT_SITE        70
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        364
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        385
FT                   /evidence="ECO:0000250"
FT   VARIANT         7
FT                   /note="N -> T"
FT   VARIANT         63
FT                   /note="D -> N"
FT   VARIANT         179
FT                   /note="L -> V"
FT   VARIANT         234
FT                   /note="N -> D"
FT   VARIANT         310..311
FT                   /note="NN -> KS"
FT   VARIANT         333
FT                   /note="A -> D"
FT   CONFLICT        373..374
FT                   /note="IV -> NG (in Ref. 2; AAA25250)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        435..449
FT                   /note="QLLPWDPMGALAFKY -> NYCHGIQWVL (in Ref. 2)"
FT                   /evidence="ECO:0000305"
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