PEPC_LACLA
ID PEPC_LACLA Reviewed; 436 AA.
AC Q9CEG3;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Aminopeptidase C;
DE EC=3.4.22.40;
DE AltName: Full=Bleomycin hydrolase;
GN Name=pepC; OrderedLocusNames=LL1878; ORFNames=L130687;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
CC -!- FUNCTION: Hydrolyzes naphthylamide-substituted amino acids as well as
CC di- and tripeptides in which the half-cystine residue is involved in a
CC disulfide loop, notably in oxytocin and vasopressin. Has also a
CC bleomycin hydrolase activity (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
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DR EMBL; AE005176; AAK05976.1; -; Genomic_DNA.
DR PIR; F86859; F86859.
DR RefSeq; NP_268035.1; NC_002662.1.
DR RefSeq; WP_010906180.1; NC_002662.1.
DR AlphaFoldDB; Q9CEG3; -.
DR SMR; Q9CEG3; -.
DR STRING; 272623.L130687; -.
DR MEROPS; C01.086; -.
DR PaxDb; Q9CEG3; -.
DR EnsemblBacteria; AAK05976; AAK05976; L130687.
DR KEGG; lla:L130687; -.
DR PATRIC; fig|272623.7.peg.2012; -.
DR eggNOG; COG3579; Bacteria.
DR HOGENOM; CLU_038600_0_1_9; -.
DR OMA; WDMIVNL; -.
DR Proteomes; UP000002196; 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; Reference proteome; Thiol protease.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..436
FT /note="Aminopeptidase C"
FT /id="PRO_0000050592"
FT ACT_SITE 68
FT /evidence="ECO:0000250"
FT ACT_SITE 356
FT /evidence="ECO:0000250"
FT ACT_SITE 378
FT /evidence="ECO:0000250"
SQ SEQUENCE 436 AA; 49914 MW; 9CDAE301CCDF0B02 CRC64;
MTVTSDFTQK LYENFAENTK LRAVENAVTK NGLLSSLEVR GSHAANLPEF SIDLTKDPVT
NQKQSGRCWM FAALNTFRHK FINEFKTEDF EFSQAYTFFW DKYEKSNWFM EQIIGDIEMD
DRRLKFLLQT PQQDGGQWDM MVAIFEKYGI VPKAVYPESQ ASSSSRELNQ YLNKLLRQDA
EILRYTIEQG GDVEAVKEEL LQEVFNFLAV TLGLPPQNFE FAFRNKDNEY KKFVGSPKEF
YNEYVGIDLN NYVSVINAPT ADKPYNKSYT VEFLGNVVGG KEVKHLNVEM DRFKKLAIAQ
MQAGETVWFG CDVGQESNRS AGLLTMDSYD FKSSLDIEFT QSKAGRLDYG ESLMTHAMVL
AGVDLDADGN STKWKVENSW GKDAGQKGYF VASDEWMDEY TYQIVVRKDL LTEEELAAYE
EKPQVLLPWD PMGALA