PEPF1_LACLC
ID PEPF1_LACLC Reviewed; 601 AA.
AC P54124; P94880;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Oligoendopeptidase F, plasmid;
DE EC=3.4.24.-;
GN Name=pepF1; Synonyms=pepF;
OS Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OG Plasmid pLP763.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1359;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=NCDO 763 / ML3;
RX PubMed=7798200; DOI=10.1016/s0021-9258(18)31602-8;
RA Monnet V., Nardi M., Chopin A., Chopin M.-C., Gripon J.-C.;
RT "Biochemical and genetic characterization of PepF, an oligopeptidase from
RT Lactococcus lactis.";
RL J. Biol. Chem. 269:32070-32076(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCDO 763 / ML3;
RX PubMed=9209029; DOI=10.1128/jb.179.13.4164-4171.1997;
RA Nardi M., Renault P., Monnet V.;
RT "Duplication of the pepF gene and shuffling of DNA fragments on the lactose
RT plasmid of Lactococcus lactis.";
RL J. Bacteriol. 179:4164-4171(1997).
CC -!- FUNCTION: Hydrolyzes peptides containing between 7 and 17 amino acids
CC with a rather wide specificity.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M3B family. {ECO:0000305}.
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DR EMBL; Z32522; CAA83534.1; -; Genomic_DNA.
DR EMBL; X99798; CAA68133.1; -; Genomic_DNA.
DR PIR; A55485; A55485.
DR AlphaFoldDB; P54124; -.
DR SMR; P54124; -.
DR MEROPS; M03.007; -.
DR BRENDA; 3.4.24.B2; 2903.
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 Gene3D; 1.10.1370.20; -; 1.
DR InterPro; IPR013647; OligopepF_N_dom.
DR InterPro; IPR042088; OligoPept_F_C.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR004438; Peptidase_M3B.
DR PANTHER; PTHR11804; PTHR11804; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR Pfam; PF08439; Peptidase_M3_N; 1.
DR TIGRFAMs; TIGR00181; pepF; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease;
KW Plasmid; Protease; Zinc.
FT CHAIN 1..601
FT /note="Oligoendopeptidase F, plasmid"
FT /id="PRO_0000078163"
FT ACT_SITE 388
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 518
FT /note="F -> S (in Ref. 2; CAA68133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 601 AA; 69675 MW; C8B5C519FFA2F787 CRC64;
MAKNRNEIPE KLTWDLTTIY KTDKEWEAEL TRIKSELSLV EETDPGHLLD SAESLLTITE
KMLSISQQVE KLYVYASMKN DQDTREAKYQ EYQSKATALY VKFGEVYAFY EPEFLKISKE
VYNKWLGELQ KLKNYDHMFE RLFAKKAHIL SQKEEKLLAA AGEIFESPSE TFEIFDNADI
KLPMVKNESD EMIQLTHGNY SSLMESKNRG VRKAAYKALY SNYEQYQHTY AKTLQTNVKV
HNLNAQIRSY DSARQAALAN NFVPEKVYDV LMEAIHQHLP LLHRYIELRK KILGITDLKM
YGIYTPLSNL GYKFNYEDGV KKAEEVLAIF GKEYKGKVKA AFEQRWIDVE ENIGKRSGAY
SGGSYDTNAF MLLNWQETLD DLFTLVHETG HSMHSAFTRE NQPYVYGNYP IFLAEIASTT
NENILTETLL KESKDDKERF ALLNHWLDSF RGTVFRQSQF AEFEQKIHEA DAAGEVLTSE
YLNSLYGEIN EKYYNLAVKG NPEIQYEWAR IPHFYYNFYV FQYATGFAAA TFLAEKVVHG
STEDRQKYLE YLKAGSSAYP LEVIAKAGVD MESTDYLDAA FELFENRLSE LEKLVEKGVH
L