ID R9IT06_9FIRM Unreviewed; 602 AA.
AC R9IT06;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=C804_04857 {ECO:0000313|EMBL:EOS24983.1};
OS Lachnospiraceae bacterium A4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=397291 {ECO:0000313|EMBL:EOS24983.1, ECO:0000313|Proteomes:UP000014118};
RN [1] {ECO:0000313|EMBL:EOS24983.1, ECO:0000313|Proteomes:UP000014118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4 {ECO:0000313|EMBL:EOS24983.1,
RC ECO:0000313|Proteomes:UP000014118};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium A4.";
RL Submitted (APR-2013) 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:EOS24983.1}.
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DR EMBL; ASSR01000115; EOS24983.1; -; Genomic_DNA.
DR AlphaFoldDB; R9IT06; -.
DR STRING; 397291.C804_04857; -.
DR PATRIC; fig|397291.3.peg.5005; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_2_0_9; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000014118; 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:UP000014118};
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 208..588
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 602 AA; 69148 MW; 5E6BD32F94A32C31 CRC64;
MSNQQNSYEK RSDVPKEYTW AMEDLYASDA EWQKDLEKVR SLLPQIETFR GQLGKSADSL
LAFLKLQDDI VVLMDKFANY ALRKADENTK NTTYQGYKDQ TMSVCVEISS ALSFAEPEIL
ELPDAVLNTF YEKQPALLPY KRSLNDILRK KAHILSDAEE KILAAAGDLA QSPEDIFGLL
NDADMTYESV SDIEGNRLAV THASFIPLMQ NYDRNVRKDA FDSLYKTYDE HKNTSAAILS
AQMKQLNFFA KMRKYNSPLE AALDQTNVNP QVYYNLIEAV HENMESMYKY VRLRKKLLKV
DELHMYDLYV PMVSNAERSI SFAETKENIR EALAVLGEDY VALLDEGFRS RWIDIYENTG
KRSGAYSCGC RVHPYVLLNY KDNLDSEFTT VHEMGHALHS YLSNKHQPIA DADYVIFVAE
VASTCNEALL MQHLLKKTTD KKERAYLINY FLEQFRTTLY RQTMFAEFEL KMSQMVQNGE
SINSESACKV YHELIDLYFG KDIVHDAKID LEWARIPHFF YNFYVYQYAT GFSAAIALSQ
KILKEGAPAV KAYKENFLSA GRSKDPVSIL KDAGVDMSTK TPVEEALKLF DSLIDEMEEL
MR
//
