ID C3GS86_BACTU Unreviewed; 605 AA.
AC C3GS86;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=bthur0010_51410 {ECO:0000313|EMBL:EEM74819.1};
OS Bacillus thuringiensis serovar pondicheriensis BGSC 4BA1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=527029 {ECO:0000313|EMBL:EEM74819.1};
RN [1] {ECO:0000313|EMBL:EEM74819.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 4BA1 {ECO:0000313|EMBL:EEM74819.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(2012).
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:EEM74819.1}.
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DR EMBL; ACNH01000100; EEM74819.1; -; Genomic_DNA.
DR RefSeq; WP_000655838.1; NZ_CM000755.1.
DR AlphaFoldDB; C3GS86; -.
DR HOGENOM; CLU_021290_1_1_9; -.
DR Proteomes; UP000006660; Chromosome.
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 213..589
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 605 AA; 69294 MW; 82E1D177515CE8CB CRC64;
MKDVIEKRHI RAEVPIELTW DLSDLYESDK EWETALRVLT DDIKKLDAFK GQLHTSPTTL
LHCLLLEEEL LMKLTKLYSY ANLKESTDRT NPVIQANSSK IAALWTKVHT ALSFIHNEIL
SLEEGTIEKY LTEETKLEPF RKSLLDILQK RQHTLSPETE EALAALGEVH SSPYKIYGMT
KLADMDFNSI QDEQGNELPV SFSLFESKYE FSPSVDIRRK AYSSFVSTLK RYKNTVATTY
ATEVKKQVTL SRLRKFESVT HMLLEPQKVP LEMYNNQLDI IYKELAPHMR RFADLKKKVL
GLDQMLFCDL HAPLDPEFNP AITYEEAGKL IQDSLQVLGD EYSAIIKKGF KERWVDLADN
VGKSTGAFCS SPYGSHPYIL ITWQNTMRGC FTLAHEFGHA GHFYLANKNQ RIMNVRPSMY
FVEAPSTMNE LLLAQHLLAT TDDKRMRRWV ILQLLGTYYH NFVTHLLEGE YQRRVYSLAE
EGEALTATTL TEIKTNVLST FWGNSVEIDE GAGLTWMRQP HYYMGLYSYT YSAGLTASTA
VAQMIKEEGQ PAVDRWLDVL RAGGTMKPLE LMKRAGVDMS KPDAIRKAVS YVGSLIDELE
RSYEE
//
