ID D4M7P1_9BACT Unreviewed; 659 AA.
AC D4M7P1;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=SY1_04390 {ECO:0000313|EMBL:CBL27886.1};
OS Fretibacterium fastidiosum.
OC Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC Fretibacterium.
OX NCBI_TaxID=651822 {ECO:0000313|EMBL:CBL27886.1, ECO:0000313|Proteomes:UP000008957};
RN [1] {ECO:0000313|EMBL:CBL27886.1, ECO:0000313|Proteomes:UP000008957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGP1 {ECO:0000313|EMBL:CBL27886.1,
RC ECO:0000313|Proteomes:UP000008957};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Wade W., Vartoukian S.;
RT "The genome sequence of Synergistetes sp. SGP1.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL27886.1, ECO:0000313|Proteomes:UP000008957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGP1 {ECO:0000313|EMBL:CBL27886.1,
RC ECO:0000313|Proteomes:UP000008957};
RA Pajon A.;
RL Submitted (MAR-2010) 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}.
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DR EMBL; FP929056; CBL27886.1; -; Genomic_DNA.
DR AlphaFoldDB; D4M7P1; -.
DR KEGG; sbr:SY1_04390; -.
DR PATRIC; fig|651822.3.peg.1925; -.
DR HOGENOM; CLU_021290_2_0_0; -.
DR BioCyc; FFAS651822:G13GF-272-MONOMER; -.
DR Proteomes; UP000008957; 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; 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:UP000008957};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..659
FT /note="Oligoendopeptidase F"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003061828"
FT DOMAIN 174..243
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 265..644
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 659 AA; 74787 MW; 64F7380392CE8614 CRC64;
MKGLRTRRAL PLLAAACFSC AGLAAGGAAA GVEKFDALTR GVVPMNFAMR FEAPEAMGDG
TGGVPERRDV PEAMRWDLEA IYPSFEAWER AFSDLTPKID ALAGFAGRLG EGPKKLLEYL
KAEEAVSLEL EKLYVYANMK SHEDLRETRP MELASRIEAL SARHGVVTAF FAPEVLELPE
DELRRWVRGE PGLKLYAFFV ERLLREREHI LPRAEEALLA SAREATAAPE NAFSLLTNAD
LKFPTIRDEE GRSVELTEER WYKLSRSPSR DVRRAAFEGI YGTYGSFKNA LAALYAGSVK
GDLFYARARR YKDSLEAALF GDNVPRSVYE NVVDTAARCA PLMHRLVALR KRALKLDRLH
YYDLNVPIAE EPREDIPYER ACRMVAEALA PLGEDYVANF KRGLAERWID VYENRGKRKG
AYSWGSYATH PYVLLNYNGT LNDVFTLAHE MGHSMHSWYS HRNQPQVYGD YTILLAEVAS
TTNEALLLGH LLKTAKTEEE RKWLLSYYYN MVRTTFFRQA MFADFELQVH ARAEEGGALT
PEWMSGLWRE LNERCYGPDM APDELLWVEW ARIPHFYSAF YVYKYVTGFT AANAFASAIL
AGEPGAVDRY LTFLKSGGSD ESLNILRRAG VDLTSREPFD RTMKLFQERL EEGERVWGR
//
