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Database: UniProt
Entry: R6H972_9ACTN
LinkDB: R6H972_9ACTN
Original site: R6H972_9ACTN 
ID   R6H972_9ACTN            Unreviewed;       605 AA.
AC   R6H972;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=BN534_00379 {ECO:0000313|EMBL:CDB34268.1};
OS   Eggerthella sp. CAG:209.
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Eggerthella.
OX   NCBI_TaxID=1262875 {ECO:0000313|EMBL:CDB34268.1, ECO:0000313|Proteomes:UP000018042};
RN   [1] {ECO:0000313|EMBL:CDB34268.1, ECO:0000313|Proteomes:UP000018042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:209 {ECO:0000313|Proteomes:UP000018042};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDB34268.1}.
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DR   EMBL; CBDM010000248; CDB34268.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6H972; -.
DR   Proteomes; UP000018042; 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; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11804:SF84; SACCHAROLYSIN; 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:UP000018042};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          114..183
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          204..584
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   605 AA;  68577 MW;  ED3FD1D9A958AC08 CRC64;
     MTTYSSREEI DEQYRWDLSS IFESDEAFLA ALEEAKKLPP RFASFQGKIS ASAADLLAYL
     KLDDEAGLIL TKLANYAERK SDEDTRESRY QDYSSQVMTL WVSLSSASSW FTSELLSLSE
     QEMEGFYSQE PELELYRRCL DAIFSRREHV LSPAEEKLLA AAGDMANQPD NIFSLLNDAD
     LTFPDAHDVE GAAHPVTHGS YIPLMMSADR TLRESAYESL YSSYRQFRNT FAATLGAQNK
     QLKFFAEARR YESALEAALS ANEVPTQVYT NLIETVHNNM DAMYKYVALR KELLDVDELR
     FSDLYVPIVD DVELTFTYEE ACDIILEALR PMGENYLALV RRGLSERWID VYETPGKRSG
     AYSAGGYGMH PVILLNFQGK LDDVFTLIHE MGHSIHTYLS CANQPVCYSD YVIFVAEVAS
     TCNEALLTRY LLDHAKNERE RAYFLNHFLE QFRATLYRQT MFAEFELKVA ELTAQGAGIT
     ADALCGIYKE LNAQYFGDGI ALDENIALEW ARIPHFYYRF YVYQYATGFA AAIALSQRIL
     DLGEQGREGY LGFLKGGSSK PPIDLLRGAG VDMLSPEPVE DALKLFDEMV DEMAEACRKL
     KAEKH
//
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