ID A0A1J0A7S6_9ENTE Unreviewed; 604 AA.
AC A0A1J0A7S6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Oligoendopeptidase {ECO:0000313|EMBL:APB31953.1};
GN ORFNames=BHY08_09105 {ECO:0000313|EMBL:APB31953.1};
OS Vagococcus teuberi.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=519472 {ECO:0000313|EMBL:APB31953.1, ECO:0000313|Proteomes:UP000191200};
RN [1] {ECO:0000313|EMBL:APB31953.1, ECO:0000313|Proteomes:UP000191200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21459 {ECO:0000313|EMBL:APB31953.1,
RC ECO:0000313|Proteomes:UP000191200};
RA Wullschleger S., Seifert C., Baumgartner S., Lacroix C., Bonfoh B.,
RA Stevens M.J., Meile L.;
RT "Vagococcus teuberi sp. nov., isolated from the Malian artisanal sour milk
RT fene.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|RuleBase:RU003435}.
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DR EMBL; CP017267; APB31953.1; -; Genomic_DNA.
DR RefSeq; WP_071457561.1; NZ_CP017267.1.
DR AlphaFoldDB; A0A1J0A7S6; -.
DR STRING; 519472.BHY08_09105; -.
DR KEGG; vte:BHY08_09105; -.
DR OrthoDB; 9769691at2; -.
DR Proteomes; UP000191200; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09607; 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; IPR034006; M3B_PepF_2.
DR InterPro; IPR013647; OligopepF_N_dom.
DR InterPro; IPR042088; OligoPept_F_C.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR011977; Pept_M3B_clade3.
DR InterPro; IPR001333; Peptidase_M32_Taq.
DR NCBIfam; TIGR02290; M3_fam_3; 1.
DR PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 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|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000191200};
KW Zinc {ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 114..183
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 203..584
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 604 AA; 69148 MW; DE33A9091FA5B8E8 CRC64;
MTYSITWDLD SIFNGGIDSK ELEQRLLLLD DEITEYQSLV TDWNPETDAP DFQTFEAIMT
VQEKLSKGFG QTISFVNAIQ SADVNNKKAG SVLAGLFTKL TGFKNANVLF NKKLTNLSTD
TWNTLLHSDF AKKQGVAFNL TEAREQSKRL LSENEESVIN QLSTDGFNAW SSHYDTIVAN
IQFPFEEDGK TTYLSAGQAF NRMMGDADKD VRQRLFDTWE KTWANYAPLF ADTLNHLDGF
RLTNNKLHGI TDHLEIPLEY NRMKKETLDA MWGTIAANKQ PFVDFLTRKA QLFGKEKMDW
QDQDAPVILG EFEEKRYTFN EAADFIIENF NKFSPKMADF AKMAFEKSWI EAEDRPGKRP
GGYCTGLPEN EESRIFMTYG ESINEVSTLA HELGHAFHSH VMWDLPSVSQ DYAMNVAETA
STFAELIVAD ATLKQAKSAE EKINLLDIKM QNATAMFMNI HARFIFENNF YTERKEKVLT
DTEITDLMVA AQKESYCDSL NSYHPHFWAS KLHFYIDDVP FYNFPYTFGY LFSLGIYAFA
QKQGTSFEDD YIALLRDTAS MTTEELAKKH LGVDLTSSEF WQAGIDMMIQ DVNTFLELTE
DYVK
//
