ID V6Z0H7_STRAG Unreviewed; 602 AA.
AC V6Z0H7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:ESV53741.1};
GN ORFNames=SAG0136_00360 {ECO:0000313|EMBL:ESV53741.1};
OS Streptococcus agalactiae LMG 14747.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1154860 {ECO:0000313|EMBL:ESV53741.1, ECO:0000313|Proteomes:UP000018482};
RN [1] {ECO:0000313|EMBL:ESV53741.1, ECO:0000313|Proteomes:UP000018482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 14747 {ECO:0000313|EMBL:ESV53741.1,
RC ECO:0000313|Proteomes:UP000018482};
RA Richards V.P., Durkin S.A.S., Kim M., Pavinski Bitar P.D., Stanhope M.J.,
RA Town C.D., Venter J.C.;
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESV53741.1}.
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DR EMBL; ANQC01000006; ESV53741.1; -; Genomic_DNA.
DR AlphaFoldDB; V6Z0H7; -.
DR eggNOG; COG1164; Bacteria.
DR Proteomes; UP000018482; 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; cd09609; 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 InterPro; IPR034009; M3B_PepF_4.
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; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11804:SF45; SIMILAR TO OLIGOENDOPEPTIDASE; 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};
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 122..175
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 199..579
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 602 AA; 68745 MW; F6AD583723E6F8EA CRC64;
MKLKKRADFP ENELWDLTAL YKDRQDFLLA IEKALGDIDT FVRDYQNNLN SVDDFTQALM
ELEQIYIQMS HIETYAFMPQ TTDFSSEEFA EIAKAGDDFA TKASVALSFF DTALATADSA
VLDELEANPH FSAAIRQAKI QKKHLLDPQV EKALSNLREV LSAPYDIYTK MRAGDFAMED
FEVDGKIYQN SFVSYENFYQ NHEDAEIREK AFRSFSKGLR AHQNAAAAAY LAKVKSEKLI
ADMRGYDSVY DYLLAEQEVD RSMFDRQINL IMAEFGPVAQ KYLKHIAEVN GLDKMTFADW
KLDIDTELNP DVSIDDAYEL VMKSVTPLGP EYIKEVERYQ TERWVDFAAN ANKDSGGYAA
DPYKVHPYVL MSWTGRMSDV YTLIHEIGHS GQFIFSDNNQ SYYNTHMSTY YVEAPSTFNE
LLLSDYLENQ FDTARQKRFA LAHRLTDTYF HNFITHLLEA AFQRKVYDLI EAGGTFGAET
LNTFMKEVLT DFWGDAVEID DDAALTWMRQ AHYYMGLYSY TYSAGLALST AGYLNLKNNA
NGAQEWLELL KSGGSKTPLD TAMIIGADIS TDKPLRDTIQ FLSDTVDQII THSQELKHDK
TQ
//