ID   PEPF2_LACLC             Reviewed;         602 AA.
AC   P94876;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Oligoendopeptidase F, chromosomal;
DE            EC=3.4.24.-;
GN   Name=pepF2;
OS   Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1359;
RN   [1]
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; X99710; CAA68044.1; -; Genomic_DNA.
DR   AlphaFoldDB; P94876; -.
DR   SMR; P94876; -.
DR   MEROPS; M03.007; -.
DR   PRIDE; P94876; -.
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.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           1..602
FT                   /note="Oligoendopeptidase F, chromosomal"
FT                   /id="PRO_0000078164"
FT   ACT_SITE        389
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         388
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         392
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         395
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   602 AA;  69991 MW;  D02235F1748B1ADF CRC64;
     MVKNRNEIPE ALTWDLTTIF STDQKWETEL EKVKKELSLV ETNDKGHLLD SAETLLTITK
     NMLSISQKVE KLYVYASMKN DQDTREAKYQ DYQSKATALY VNFGESYAFY EPEFLKNLQK
     ETYGKWLETL QELKNYDHMF ERLFAKKEHI LSQKEGKILA APGEIFESPS ETFEIFDNAD
     VKFPFVKNEL GEKIQLTHGN YGSLMESENR EVRKAAYEAL YSNYEQCQHT YAKTLQTNVK
     VHNFNAQIRA YDSARQAALM SNFVPEKVYD VLIEGIHQHL PLLHRYIELR KKILEISDFK
     MYDIYTPLSN LDYKFNYTEG VKKAQEVLAI FGEEYSQKVK AAFDERWIDV EENVGKRSGA
     YSGGSYDTKA FMLLNWQGTL DDLFTLVHEM GHSIHSTFTR ENQPYVYGDY PIFLAEIAST
     TNENILTETL LKESNDEKER FALLNHWLDS FRGTVFRQSQ FAEFEQKIHE VDAEGEVLTS
     EFLNSLYGEL NEKYYGLSAK ENPEIQFEWA KIPHFYYNFY VFQYATGFSA ASFIAEKVVH
     GSVTDRQNYL DYLKAGSSAY PLDVIAKAGV NMESTDYLES AFKLFEKRLN ELEKLVEKGV
     HL