ID B9IT15_BACCQ Unreviewed; 605 AA.
AC B9IT15;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN OrderedLocusNames=BCQ_5303 {ECO:0000313|EMBL:ACM15703.1};
OS Bacillus cereus (strain Q1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=361100 {ECO:0000313|EMBL:ACM15703.1, ECO:0000313|Proteomes:UP000000441};
RN [1] {ECO:0000313|EMBL:ACM15703.1, ECO:0000313|Proteomes:UP000000441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q1 {ECO:0000313|EMBL:ACM15703.1,
RC ECO:0000313|Proteomes:UP000000441};
RX PubMed=19060151; DOI=10.1128/JB.01629-08;
RA Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA Xue Y., Zhu Y., Jin Q.;
RT "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT with industrial applications.";
RL J. Bacteriol. 191:1120-1121(2009).
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}.
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DR EMBL; CP000227; ACM15703.1; -; Genomic_DNA.
DR AlphaFoldDB; B9IT15; -.
DR KEGG; bcq:BCQ_5303; -.
DR HOGENOM; CLU_021290_1_1_9; -.
DR Proteomes; UP000000441; 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 212..589
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 605 AA; 69174 MW; BC41915BCCF6FE28 CRC64;
MKDVIEKRYI RAEVPTELTW DLSDLYESDK EWETALRVLT DDIKKLDAFK GQLHNSPTTL
LHCLLLEEEL LMKLTKLYSY ANLKESTDRT NPVIQANSSK IAALWTKVHT ALSFIHNEIL
SLEEGTIEKY LTEETKLEPF RKSLLDILQK RPHTLSPETE EALAALGEVH SSPYKIYGMT
KLADMDFNSI QDEQGNELPV SFALFESKYE FSPSADIRRK AYSSFVSTLK RYKNTVATTY
ATEVKKQVTL SRLRKFESVT HMLLEPQKVP LEMYNNQLDI IYKELAPHMR RFADLKKKVL
GLDEMLFCDL HAPLDPEFNP TITYEEAGKL IQDSLQVLGD EYSSIIEKGF KERWVDLADN
VGKSTGAFCS SPYGSHPYIL ITWQNTMRGC FTLAHEFGHA GHFYLANKNQ RIMNVRPSMY
FVEAPSTMNE LLLAQHLLAT NDDKRMRRWV ILQLLGTYYH NFVTHLLEGE YQRRVYSLAE
EGGALTATTL TEIKANVLST FWGDSVKIDE GAGLTWMRQP HYYMGLYSYT YSAGLTASTA
VAQMIKEEGQ PAVDRWLDVL RAGGTMKPLE LMKHAGVDMS KPDTIRRAVS YVGSLIDELE
SSYQE
//
