ID A6NRD9_9FIRM Unreviewed; 600 AA.
AC A6NRD9;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN Name=pepF {ECO:0000313|EMBL:EDN01635.1};
GN ORFNames=BACCAP_00767 {ECO:0000313|EMBL:EDN01635.1};
OS Pseudoflavonifractor capillosus ATCC 29799.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Pseudoflavonifractor.
OX NCBI_TaxID=411467 {ECO:0000313|EMBL:EDN01635.1, ECO:0000313|Proteomes:UP000003639};
RN [1] {ECO:0000313|EMBL:EDN01635.1, ECO:0000313|Proteomes:UP000003639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDN01635.1,
RC ECO:0000313|Proteomes:UP000003639};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDN01635.1, ECO:0000313|Proteomes:UP000003639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDN01635.1,
RC ECO:0000313|Proteomes:UP000003639};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Pseudoflavonifractor capillosus ATCC 29799.";
RL Submitted (JUN-2007) 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:EDN01635.1}.
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DR EMBL; AAXG02000005; EDN01635.1; -; Genomic_DNA.
DR RefSeq; WP_006571316.1; NZ_AAXG02000005.1.
DR AlphaFoldDB; A6NRD9; -.
DR STRING; 411467.BACCAP_00767; -.
DR eggNOG; COG1164; Bacteria.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000003639; 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:UP000003639};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 115..184
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 205..585
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 600 AA; 68164 MW; EC1EF775236E12C6 CRC64;
MAHTLPTRSQ VDPANTWAIT DLYPSDQAWR EACENVRGLV RDLAAYRGRL GESAATLLAF
LRLQDEIDLQ GDRMISYAFR KSDEDTRNPV YQEMSAQAQN FLVELSQALS FQTPELLAIE
DATLESFYEQ EPALAHYRLM LKRIRSRKDH TLSPDCEALL ASAERMGQAP DDIFSLLNDA
DMTYPDATDS KGETHPVTHG NYVALLQSAD RTLRQSAFQS LYSVYGQFRN TCAAILGAQM
KQLQFFADAR RYPSALHAAL AETEVDPQIY HNLIQTVHDN LDAMHRYVRL RKKLLGVDKL
HYYDLYTPIV ADEDASIPFE QAKDMAREAL KPLGEDYLKI LNEGFDNRWI DVYENQGKRS
GAYSAGVYGV HPYVLLNYTD TLDDVFTLVH EMGHALHSYL SNHTQSVTYA GYKIFVAEVA
STCNEALLMQ HLLSKTTEPK CRAYLINHFL EQFRGTLYRQ TMFAEFELWC SEQTRKGQPL
TAESLNEKYA ELNRLYYGED IEPDPEIALE WARIPHFYYN FYVYQYATGF TSAIALSQRI
LKEGRPAVED YLRFLSGGCS ADPVSLLKGA GVDISSPAPI VDALKLFDTL IGEMEQLMQS
//
