ID   A0A0N1EJS0_9SPHN        Unreviewed;       601 AA.
AC   A0A0N1EJS0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=ADT71_15710 {ECO:0000313|EMBL:KPH62383.1};
OS   Novosphingobium sp. ST904.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1684385 {ECO:0000313|EMBL:KPH62383.1, ECO:0000313|Proteomes:UP000037878};
RN   [1] {ECO:0000313|EMBL:KPH62383.1, ECO:0000313|Proteomes:UP000037878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST904 {ECO:0000313|EMBL:KPH62383.1,
RC   ECO:0000313|Proteomes:UP000037878};
RA   Thijs S., Bottos E.M., Van Hamme J.D., Gkorezis P., Rineau F.,
RA   Vangronsveld J.;
RT   "Novosphingobium nitrophenolicus strain ST904 degrades p-nitrophenol and
RT   stimulates plant growth.";
RL   Submitted (JUL-2015) 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:KPH62383.1}.
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DR   EMBL; LGJH01000149; KPH62383.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1EJS0; -.
DR   STRING; 1684385.ADT71_15710; -.
DR   PATRIC; fig|1684385.3.peg.1873; -.
DR   Proteomes; UP000037878; 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; cd09608; 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   Gene3D; 1.10.287.830; putative peptidase helix hairpin domain like; 1.
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:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 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   Reference proteome {ECO:0000313|Proteomes:UP000037878};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          116..184
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          209..583
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   601 AA;  67241 MW;  EBA82AE37E91D4D3 CRC64;
     MPGLASSAAA ATNDLAAWDL TDLYPDLASW ETARKQVMDA LPRLAAYKGM LGQSAEAMAK
     VLEDISAVTL KAIRVYTYAA LKADEDLRIA PNQERQAQVQ DMFAAFGEAT AWTSPEILAA
     GKDKVERFIA SNDALKRRFA FSLRNTLRKA DHTLDTQGEQ ILAAASSPLS GPGTIREQLF
     NSDIPWPTIT LSDGRETRLD SQGYSLTRDA ANREDRKKVF DAYFGEMGKF ESSLGAAMAA
     KLKGDVFEAR IRKYPNSLAM AQADDDVPET VYRTLVSATN EGLPQLHRYF QLRRKMLKLP
     DIHYYDIYPP LVSLDRKFTL ADMRNITLKA VAPLGPDYVK QLGEATAARW MDPLPRPGKT
     SGAYMNGSVY DVHPYLLLNL GENYEGLSTY AHEWGHAMHS LLAKSAQPFE LADYPTFTAE
     IASTCNELLL TDYMLDQAKT KQERIYYLGM RLEGLRGTYF RQTMFAEFEL KMHEMAEAGQ
     GLSGESLTRV YLDLLKRYHG PDFVIDEPYA IEWAYIPHFF SFFYVYQYAT SITAGTWFAN
     AILKGGNTER ERYLDVLRAG GSDHPTAILK RAGLDMTSPQ PYRDLIAGFG QTIDEIESLL
     G
//