ID   PEPC_LISIN              Reviewed;         441 AA.
AC   Q928V0;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Aminopeptidase C;
DE            EC=3.4.22.40;
DE   AltName: Full=Bleomycin hydrolase;
GN   Name=pepC; OrderedLocusNames=lin2432;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL596172; CAC97659.1; -; Genomic_DNA.
DR   PIR; AC1736; AC1736.
DR   RefSeq; WP_010991187.1; NC_003212.1.
DR   AlphaFoldDB; Q928V0; -.
DR   SMR; Q928V0; -.
DR   STRING; 272626.lin2432; -.
DR   MEROPS; C01.086; -.
DR   EnsemblBacteria; CAC97659; CAC97659; CAC97659.
DR   KEGG; lin:pepC; -.
DR   eggNOG; COG3579; Bacteria.
DR   HOGENOM; CLU_038600_0_1_9; -.
DR   OMA; WDMIVNL; -.
DR   OrthoDB; 1064956at2; -.
DR   Proteomes; UP000002513; Chromosome.
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; Hydrolase; Protease; Thiol protease.
FT   CHAIN           1..441
FT                   /note="Aminopeptidase C"
FT                   /id="PRO_0000050594"
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;  50599 MW;  365F909E54570B63 CRC64;
     MSTEITFDQL ESFSKKWREN PDKLVFQASI MKNGIKAATE NPVSKATVQP VFSHEVHTDK
     VSNQQQSGRC WMFAALNTFR HKLNGTLGLK DFELSQNYTN FWDKLEKANY FLENIIETAN
     EDEDSRLVSW LLDTPQQDGG QWDMLVSIIE KYGVVSKSAM PETFQSSKSA DLNHLLNERL
     RTDAVILRKA VKEQKDTAGL KEEMLAEVYQ LLVMTLGEPP KVFDFEYRNK DNEFKQDLQI
     TPKEFYKRYV DMDLKDYIPL INAPTKDKPF NQAFTVDYLG NIVNGTPIKY LNVEMDVLKK
     ATADQIKDGE TVWFGCDVGQ LSERTTGIMD TDIFLLNQAF GFKTAMTKAE RLDYKHSMLT
     HAMVLTGVNI VNNEVNRWKV ENSWGEKIGN NGYFVASDAW MDEFTFQVVV HKKYLSKELI
     EAFSNEPIAL KPWDPMGSLA L