ID Q02VB4_LACLS Unreviewed; 604 AA.
AC Q02VB4;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN OrderedLocusNames=LACR_D12 {ECO:0000313|EMBL:ABJ74108.1};
OS Lactococcus lactis subsp. cremoris (strain SK11).
OG Plasmid pLACR4 {ECO:0000313|Proteomes:UP000000240}.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=272622 {ECO:0000313|EMBL:ABJ74108.1, ECO:0000313|Proteomes:UP000000240};
RN [1] {ECO:0000313|EMBL:ABJ74108.1, ECO:0000313|Proteomes:UP000000240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK11 {ECO:0000313|EMBL:ABJ74108.1,
RC ECO:0000313|Proteomes:UP000000240};
RC PLASMID=Plasmid pLACR4 {ECO:0000313|Proteomes:UP000000240};
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA Kozyavkin S., Weimer B., Mills D.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC -!- FUNCTION: Has oligopeptidase activity and degrades a variety of small
CC bioactive peptides. {ECO:0000256|RuleBase:RU368091}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU368091};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU368091};
CC -!- SIMILARITY: Belongs to the peptidase M3B family.
CC {ECO:0000256|RuleBase:RU368091}.
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DR EMBL; CP000429; ABJ74108.1; -; Genomic_DNA.
DR AlphaFoldDB; Q02VB4; -.
DR MEROPS; M03.007; -.
DR KEGG; llc:LACR_D12; -.
DR HOGENOM; CLU_021290_2_0_9; -.
DR Proteomes; UP000000240; Plasmid pLACR4.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09608; M3B_PepF; 1.
DR Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR Gene3D; 1.10.287.830; putative peptidase helix hairpin domain like; 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 NCBIfam; TIGR00181; pepF; 1.
DR PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR Pfam; PF08439; Peptidase_M3_N; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368091};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU368091};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU368091}; Plasmid {ECO:0000313|EMBL:ABJ74108.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU368091};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 116..184
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 206..585
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 604 AA; 70228 MW; B780DDF5B81FE978 CRC64;
MSFMAKNRNE IPEKLTWDLT TIYKTDKEWE AELTRIKSEL SLVEETDPGH LLDSAESLLT
ITEKMLSISQ QVEKLYVYAS MKNDQDTREA KYQEYQSKAT ALYVKFGEVY AFYEPEFLKI
SKEVYNKWLG ELQKLKNYDH MFERLFAKKA HILSQKEEKL LAAAGEIFES PSETFEIFDN
ADIKLPMVKN ESDEMIQLTH GNYSSLMESK NRGVRKAAYK ALYSNYEQYQ HTYAKTLQTN
VKVHNLNAQI RSYDSARQAA LANNFVPEKV YDVLMEAIHQ HLPLLHRYIE LRKKILGITD
LKMYDIYTPL SNLDYKFNYE DGVKKAEEVL AIFGKEYKGK VKAAFEQRWI DVEENIGKRS
GAYSGGSYDT NAFMLLNWQE TLDDLFTLVH ETGHSMHSAF TRENQPYVYG NYPIFLAEIA
STTNENILTE TLLKESKDDK ERFALLNHWL DSFRGTVFRQ SQFAEFEQKI HEADAAGEVL
TSEYLNSLYG EINEKYYNLA VKENPEIQYE WARIPHFYYN FYVFQYATGF AAATFLAEKV
VHGSTEDRQK YLEYLKAGSS AYPLEVIAKA GVDMESTDYL DAAFELFENR LSELEKLVEK
GVHL
//
