PEPF_LACLA
ID PEPF_LACLA Reviewed; 601 AA.
AC Q9CEV7;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Oligoendopeptidase F homolog;
DE EC=3.4.24.-;
GN Name=pepF; OrderedLocusNames=LL1727; ORFNames=L166370;
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 peptides containing between 7 and 17 amino acids
CC with a rather wide specificity. {ECO:0000250}.
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 M3 family. {ECO:0000305}.
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DR EMBL; AE005176; AAK05825.1; -; Genomic_DNA.
DR PIR; G86840; G86840.
DR RefSeq; NP_267883.1; NC_002662.1.
DR RefSeq; WP_010906109.1; NC_002662.1.
DR AlphaFoldDB; Q9CEV7; -.
DR SMR; Q9CEV7; -.
DR STRING; 272623.L166370; -.
DR MEROPS; M03.007; -.
DR PaxDb; Q9CEV7; -.
DR EnsemblBacteria; AAK05825; AAK05825; L166370.
DR KEGG; lla:L166370; -.
DR PATRIC; fig|272623.7.peg.1852; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_2_0_9; -.
DR OMA; YRQTMFA; -.
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 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; Reference proteome;
KW Zinc.
FT CHAIN 1..601
FT /note="Oligoendopeptidase F homolog"
FT /id="PRO_0000078162"
FT ACT_SITE 388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 391
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 601 AA; 69884 MW; 045E6873F10FE19A CRC64;
MAKNRNEITE KLTWDLTTIY KTDKEWEAEL TRIKSELSLV EETDPGHLLD SAESLLTITE
KMLSISQQVE KLYVYASMKN DQDTREAKYQ EYQSKATALY VKFGEVYAFY EPEFLKISKE
VYNKWLGELQ KLKNYDHMFE RLFAKKAHIL SQKEEKLLAA AGEIFESPSE TFEIFDNADI
KLPMVKNESD EMIQLTHGNY SSLMESKNRG VRKAAYKALY SNYEQYQHTY AKTLQTNVKV
HNLKAQIRSY DSARQAALAN NFVPEKVYDV LMEAIHQHLP LLHRYIELRK KILGITDLKM
YDIYTPLSNL DYKFNYEDGV KKAEEVLAIF GKEYKGKVKA AFEQRWIDVE ENIGKRSGAY
SGGSYDTNAF MLLNWQETLD DLFTLVHEMG HSMHSAFTRE NQPYVYGDYP IFLAEIASTT
NENILTETLL KESKDDKERF ALLNHWLDSF RGTVFRQSQF AEFEQKIHEA DAAGEVLTSE
YLNSLYGEIN EKYYNLAAKE NPEIQYEWAR IPHFYYNFYV FQYATGFAAA TFLAEKVVHG
STEDRQKYLE YLKAGSSAYP LEVIAKAGVD MESTDYLDAA FELFENRLSE LEKLVEKGVH
L