ID   A0A0A8JN53_BACSX        Unreviewed;       601 AA.
AC   A0A0A8JN53;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=OXB_3387 {ECO:0000313|EMBL:BAQ11856.1};
OS   Bacillus sp. (strain OxB-1).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=98228 {ECO:0000313|EMBL:BAQ11856.1, ECO:0000313|Proteomes:UP000031651};
RN   [1] {ECO:0000313|Proteomes:UP000031651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OxB-1 {ECO:0000313|Proteomes:UP000031651};
RA   Yamaguchi T., Asano Y.;
RT   "Complete genome of an aldoxime degrader Bacillus sp. OxB-1.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAQ11856.1, ECO:0000313|Proteomes:UP000031651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OxB-1 {ECO:0000313|EMBL:BAQ11856.1,
RC   ECO:0000313|Proteomes:UP000031651};
RA   Yamaguchi T., Asano Y.;
RT   "Complete Genome Sequence of an Aldoxime Degrader, Bacillus sp. OxB-1.";
RL   Genome Announc. 3:e00025-15(2015).
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; AP013294; BAQ11856.1; -; Genomic_DNA.
DR   RefSeq; WP_041075739.1; NZ_AP013294.1.
DR   AlphaFoldDB; A0A0A8JN53; -.
DR   STRING; 98228.OXB_3387; -.
DR   KEGG; baco:OXB_3387; -.
DR   HOGENOM; CLU_021290_1_1_9; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000031651; 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   Coiled coil {ECO:0000256|SAM:Coils};
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   Reference proteome {ECO:0000313|Proteomes:UP000031651};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          114..180
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          203..582
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
FT   COILED          18..45
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   601 AA;  68105 MW;  52577AD3B638C758 CRC64;
     MKTLPARSEV NEKDTWNLAD LFKTEEDYEQ AIADLEQEVG RFAEQFEGRI DNPTIINEAL
     GKYRGIMEKF IPAATYASLA SSVDQTDDTA QLRESRFGTF AAKLSETLSF VSSELSALPA
     ETLTEAAAQS EGHARYLKQI IRKKPHQLHP EAEKTLAAFS ATFNAPYGLY NVTKLVDMTF
     GDFVAGGESY PLSYVTFEGG WESEPDTAKR RAAFDAFSAK LKEYQHTTAK TYDMHVQMEK
     TTSDLRGYEN IFDYLLMDQE VDRSMYNRQI DLIMEELAPH MRKYAKLLQK VHRLDTMTFA
     DLKIPLDPTY EPKITFEESK RYMDDALSIM GKDYAAMVDK AYEERWIDHA QNLGKSTGAF
     CSSPYGNHSY ILISWTGSME DVFVLAHELG HAGHFHYTNS EQNIFNADPS LYFIEAPSTL
     NEMLMASHLL KNSDDPKFKR WVISSIVSRT YYHNFVTHLL EAAYQRKVYE RVDGGGNVNA
     TILNGLKHEV LEEFWGDAVV INEGAELTWM RQPHYYMGLY PYTYSAGLTI STQVSERILQ
     EGQPAVDDWL NVLKAGGTKT PAELSQMAGV DITTEEPLKK TIAYIGSLID ELIQLTEQIE
     A
//