ID   PEPC_LISMO              Reviewed;         441 AA.
AC   O69192;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Aminopeptidase C;
DE            EC=3.4.22.40;
DE   AltName: Full=Bleomycin hydrolase;
GN   Name=pepC; OrderedLocusNames=lmo2338;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=V7;
RX   PubMed=11204766; DOI=10.1023/a:1026549118087;
RA   Winters D.K., Ivey D.M., Maloney T.P., Johnson M.G.;
RT   "Characterization by molecular cloning and sequencing of the gene encoding
RT   an aminopeptidase from Listeria monocytogenes.";
RL   Antonie Van Leeuwenhoek 78:141-151(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
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DR   EMBL; AF067409; AAC17920.1; -; Genomic_DNA.
DR   EMBL; AL591983; CAD00416.1; -; Genomic_DNA.
DR   PIR; AB1367; AB1367.
DR   RefSeq; NP_465861.1; NC_003210.1.
DR   RefSeq; WP_003731859.1; NZ_CP023861.1.
DR   AlphaFoldDB; O69192; -.
DR   SMR; O69192; -.
DR   STRING; 169963.lmo2338; -.
DR   MEROPS; C01.086; -.
DR   PaxDb; O69192; -.
DR   PRIDE; O69192; -.
DR   EnsemblBacteria; CAD00416; CAD00416; CAD00416.
DR   GeneID; 984466; -.
DR   KEGG; lmo:lmo2338; -.
DR   PATRIC; fig|169963.11.peg.2395; -.
DR   eggNOG; COG3579; Bacteria.
DR   HOGENOM; CLU_038600_0_1_9; -.
DR   OMA; WDMIVNL; -.
DR   PhylomeDB; O69192; -.
DR   BioCyc; LMON169963:LMO2338-MON; -.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0008234; F:cysteine-type peptidase activity; IBA:GO_Central.
DR   GO; GO:0043418; P:homocysteine catabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0009636; P:response to toxic substance; IBA:GO_Central.
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; Hydrolase; Protease; Reference proteome; Thiol protease.
FT   CHAIN           1..441
FT                   /note="Aminopeptidase C"
FT                   /id="PRO_0000050595"
FT   ACT_SITE        70
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        361
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        382
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   441 AA;  50605 MW;  A498E522451B856B CRC64;
     MQTELTFEQL ENFSRKWREN PDKLVFQASI MKNGIKAATE NPTSKVSIQP VFSHEVATDK
     VSNQQQSGRC WMFAALNTFR HKLNGTLGLK DFELSQNYTN FWDKLEKANY FLENIIETAS
     EDEDSRLVSW LLDTPQQDGG QWDMLVSIIE KYGVVPKSAM PETFQSGKSA DLNHLLNERL
     RTDAVILRKA FTEKKDTAGL KEEMLAEIYQ LLVMTLGEPP KVFDFEYRNK DNEFKQELQI
     TPKDFYERYV DMDLKNYIPL INAPTKDKPF NQAFTVDYLG NIVNGTPIKY LNVEMDVLKK
     AATDQIKDGE TVWFGCDVGQ LSEKTTGIMD TDIFLLNQTF GFKTAMTKAE RLDYKHSMLT
     HAMVLTGVNV ANGEVNRWKV ENSWGEKIGN NGYFVASDAW MDEFTFQVVV HKKYLSKELI
     EAFNQEPIAL KPWDPMGSLA L