PEPO_LACLA
ID PEPO_LACLA Reviewed; 627 AA.
AC Q07744;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Neutral endopeptidase;
DE EC=3.4.24.-;
DE AltName: Full=Endopeptidase O;
GN Name=pepO; OrderedLocusNames=LL1803; ORFNames=L49741;
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 [GENOMIC DNA].
RC STRAIN=SSL135;
RX PubMed=8244921; DOI=10.1128/jb.175.23.7523-7532.1993;
RA Tynkkynen S., Buist G., Kunji E., Kok J., Poolman B., Venema G.,
RA Haandrikman A.;
RT "Genetic and biochemical characterization of the oligopeptide transport
RT system of Lactococcus lactis.";
RL J. Bacteriol. 175:7523-7532(1993).
RN [2]
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: Endopeptidase with broad substrate specificity for several
CC oligopeptides.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0-6.5.;
CC Temperature dependence:
CC Optimum temperature is 30-38 degrees Celsius.;
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01233, ECO:0000305}.
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DR EMBL; L18760; AAA16168.1; -; Unassigned_DNA.
DR EMBL; AE005176; AAK05901.1; -; Genomic_DNA.
DR PIR; C86850; C86850.
DR PIR; F53290; F53290.
DR RefSeq; NP_267960.1; NC_002662.1.
DR RefSeq; WP_010906145.1; NC_002662.1.
DR AlphaFoldDB; Q07744; -.
DR SMR; Q07744; -.
DR STRING; 272623.L49741; -.
DR MEROPS; M13.004; -.
DR PaxDb; Q07744; -.
DR EnsemblBacteria; AAK05901; AAK05901; L49741.
DR KEGG; lla:L49741; -.
DR PATRIC; fig|272623.7.peg.1931; -.
DR eggNOG; COG3590; Bacteria.
DR HOGENOM; CLU_006187_7_2_9; -.
DR OMA; FGWAQVW; -.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd08662; M13; 1.
DR Gene3D; 1.10.1380.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR000718; Peptidase_M13.
DR InterPro; IPR018497; Peptidase_M13_C.
DR InterPro; IPR042089; Peptidase_M13_dom_2.
DR InterPro; IPR008753; Peptidase_M13_N.
DR PANTHER; PTHR11733; PTHR11733; 1.
DR Pfam; PF01431; Peptidase_M13; 1.
DR Pfam; PF05649; Peptidase_M13_N; 1.
DR PRINTS; PR00786; NEPRILYSIN.
DR PROSITE; PS51885; NEPRILYSIN; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..627
FT /note="Neutral endopeptidase"
FT /id="PRO_0000078230"
FT DOMAIN 1..627
FT /note="Peptidase M13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT ACT_SITE 476
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 539
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT BINDING 475
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 479
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 535
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT CONFLICT 76
FT /note="T -> A (in Ref. 1; AAA16168)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="S -> N (in Ref. 1; AAA16168)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="A -> V (in Ref. 1; AAA16168)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="E -> K (in Ref. 1; AAA16168)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="T -> A (in Ref. 1; AAA16168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 627 AA; 71538 MW; 940A121EC8BADF26 CRC64;
MTRIQDDLFA TVNAEWLENA EIPADKPRIS AFDELVLKNE KNLAKDLADL SQNLPTDNPE
LLEAIKFYNK AGDWQTREKA DFSAVKNELA KVETLNTFED FKNNLTQLVF HSQAPLPFSF
SVEPDMKDAI HYSLGFSGPG LILPDTTYYN DEHPRKKELL DFWAKNTSEI LKTFDVENAE
EIAKSALKFD ALLVPSANTS EEWAKYAELY HPISTDSFVS KVKNLDLKSL IKDLVKTEPD
KVIVYEDRFY ESFDSLINEE NWSLIKAWML TKIARGATSF FNEDLRILGG AYGRFLSNVQ
EARSQEKHQL DLTESYFSQV IGLFYGKKYF GEAAKADVKR MVTAMIKVYQ ARLSKNEWLS
QETAEKAIEK LDAITPFIGF PDKLPEIYSR LKTTSGSLYE DALKFDEILT ARTFEKFSED
VDKTSWHMPA HMVNAYYSPD SNTIVFPAAI LQAPFYSLEQ SSSQNYGGIG TVIAHEISHA
FDNNGAQFDK EGNLNKWWLD EDYEAFEEKQ KEMIALFDGV ETEAGPANGK LIVSENIADQ
GGITAALTAA KDEKDVDLKA FFSQWAKIWR MKASKEFQQM LLSMDVHAPA KLRANIPPTN
LEEFYETFDV KETDKMYRAP ENRLKIW
