ID E9DLU3_9STRE Unreviewed; 601 AA.
AC E9DLU3;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:EFX54479.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:EFX54479.1};
GN Name=pepF {ECO:0000313|EMBL:EFX54479.1};
GN ORFNames=HMPREF0848_00074 {ECO:0000313|EMBL:EFX54479.1};
OS Streptococcus sp. C150.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=435842 {ECO:0000313|EMBL:EFX54479.1, ECO:0000313|Proteomes:UP000005993};
RN [1] {ECO:0000313|EMBL:EFX54479.1, ECO:0000313|Proteomes:UP000005993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C150 {ECO:0000313|EMBL:EFX54479.1,
RC ECO:0000313|Proteomes:UP000005993};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D.,
RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C.,
RA Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S., Surette M.G.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptococcus sp. C150.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; GL698449; EFX54479.1; -; Genomic_DNA.
DR RefSeq; WP_008533912.1; NZ_GL698449.1.
DR AlphaFoldDB; E9DLU3; -.
DR MEROPS; M03.007; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_2_0_9; -.
DR Proteomes; UP000005993; Unassembled WGS sequence.
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; 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 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EFX54479.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 112..181
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 202..581
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 601 AA; 68815 MW; 75B2A52EB012C080 CRC64;
MSDNRSHLEE KYTWDLTTIF ATDAAWEAEY ESTVQDLKKA SAFAGHLLDS AKNLLEATEL
YMSLMRRLEK IYVYASMKND QDTTVGLYQE YQAKASNLYS QLSEAFAYFE PEFMALDGEK
LAAFKEQEPG LGLYDHYFER LLANKDHVLS QEAEGLLAAA GDIFNGPTET FNVLDNADIL
FPWVSDGQGD VIELTHGNFI TLMESKDRDI RKGAYEAMYG TYEQFQHTYA QTLQGVVKVH
NYQAKVRHYN SARHAALAAN FIPESVYDSL LESVHKHLPL LHRYLDLRKK VLGLDELKMY
DVYTPLSETE TALTYEESLK KAEEVLAIFG EEYSEGVHAA FTERWIDVHP NKGKRSGAYS
GGAYDTNAFM LLNWQDTLDN LFTLVHETGH SLHSTFTRKT QPYVYGDYPI FLAEIASTTN
ENILTETLLK EVKDDKTRFA ILNHFLDGFK GTVFRQTQFA EFEHAIHEAD ASGQILTADF
MNKLYADLNE KYYNLKAEDN YEIQFEWERI PHFYMNYYVY QYATGFAAAS YLAEKIVHGT
EEDKEAYLTY LKAGSSDYPL EVIKKAGVDM TNTDYLDAAF KVFEDRLVEL EALVEKGVHL
S
//
