ID J8Y7N8_BACCE Unreviewed; 605 AA.
AC J8Y7N8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=IG3_04588 {ECO:0000313|EMBL:EJV77998.1};
OS Bacillus cereus HuA2-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1053201 {ECO:0000313|EMBL:EJV77998.1, ECO:0000313|Proteomes:UP000004136};
RN [1] {ECO:0000313|EMBL:EJV77998.1, ECO:0000313|Proteomes:UP000004136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HuA2-1 {ECO:0000313|EMBL:EJV77998.1,
RC ECO:0000313|Proteomes:UP000004136};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA Swiecicka I., Hansen B.M., Andrup L., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus cereus HuA2-1.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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:EJV77998.1}.
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DR EMBL; AHDV01000035; EJV77998.1; -; Genomic_DNA.
DR RefSeq; WP_002068770.1; NZ_JH804673.1.
DR AlphaFoldDB; J8Y7N8; -.
DR PATRIC; fig|1053201.3.peg.4684; -.
DR HOGENOM; CLU_021290_1_1_9; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000004136; Unassembled WGS sequence.
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; 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 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};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU368091};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 118..187
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 212..589
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 605 AA; 68878 MW; 007F092A2911D051 CRC64;
MKNVIEKRLI RAEVSTELTW DLSDLYESDK EWETALRVLT DDIKKLDAFK GQLHTSPATL
LNCLLLEEEL LMKLTKLGAY ANLKESVDRT DSVIQANSSK ISALGTNVHT ALSFIHNEIL
SFEEGTIEKY LTEEIKLEPF RKSLLEILKK RQHTLSPETE EALAALGEVH SSPYKIYGMT
KLADMDFPSI QDEQGNDLPV SFALFESKYE FSPSAYIRKK AYSSFVSTLK RYKNTVATTY
ATEVKKQVAL SRLRKYESVT HMLLEPQKVP LEMYNNQLDI IYNELAPHMR RFADLKKNVL
GLDQMLFCDL HAPLDPEFNP TITYEEAGKL IQDSLKVLGN EYSSIIEKGF KERWVDLADN
VGKSTGAFCS SPYGSHPYIL ITWQGTMRGC FTLAHEFGHA GHFYLANKNQ RIMNVRPSMY
FVEAPSTMNE LLLAQHLLAT TEDKRMRRWV ILQLLGTYYH NFVTHLLEGE YQRRVYALAE
EGQALTATTL TEIKTKVLST FWGDSVEIDE GAGLTWMRQP HYYMGLYSYT YSAGLTASTA
VAQMIKEEGQ PAVDRWLDVL RAGGTMKPLE LMKHAGVDMS KPDAIRKAVS YVGSLIDELE
RSYQE
//
