ID F1VXE4_9BURK Unreviewed; 621 AA.
AC F1VXE4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=IMCC9480_2064 {ECO:0000313|EMBL:EGF32726.1};
OS Oxalobacteraceae bacterium IMCC9480.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae.
OX NCBI_TaxID=937450 {ECO:0000313|EMBL:EGF32726.1, ECO:0000313|Proteomes:UP000004494};
RN [1] {ECO:0000313|EMBL:EGF32726.1, ECO:0000313|Proteomes:UP000004494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC9480 {ECO:0000313|EMBL:EGF32726.1,
RC ECO:0000313|Proteomes:UP000004494};
RX PubMed=21572000; DOI=10.1128/JB.05088-11;
RA Oh H.M., Lee K., Jang Y., Kang I., Kim H.J., Kang T.W., Kim S.Y., Cho J.C.;
RT "Genome sequence of strain IMCC9480, a xanthorhodopsin-bearing
RT betaproteobacterium isolated from the Arctic Ocean.";
RL J. Bacteriol. 193:3421-3421(2011).
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:EGF32726.1}.
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DR EMBL; AEPR01000177; EGF32726.1; -; Genomic_DNA.
DR AlphaFoldDB; F1VXE4; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000004494; 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:UP000004494};
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..621
FT /note="Oligoendopeptidase F"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003276815"
FT DOMAIN 131..198
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 225..601
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 621 AA; 69076 MW; CEF085788AC4DBBD CRC64;
MFQRILRIFP ALPVLLLAAS SASAATDAFN PRWNLADLYP SAAAWQADAA KADTQINTFA
NCRGHLGDNV RRFRQCLELR ADLDKRYERL ALYANEFHAE DTGNTAGLEL TQQAEVLGAR
LEESGSFFRP ELLQLGAKKI NGFLHADKAL AIFRHPIDNL LRAVPHTLDA KGEALIATYG
LAGNSAQSVY SILTNADMPW PKVTLSDGQE VTLDQSGYTR YRGVDNRADR SKVFDAFWGK
WHEFERTFGV TFYEKLKKDT VDAKVRNYPD SITKALDANK IPVAVYDTLI AQTNANLPTL
HRYFRLRAKL LGITDMGYQD ISPPLVKGDF TYPIAQGNAL MLAAVKPLGG DYVKALEKGV
ASRWMDVYPR ARKLSGAHMA GDAYDVHPYI LLNYNDDYES VSTLAHEWGH GMHTVLANQA
QPYVTAGYPI FTAEIASTTN ESLLLAHMLA VSKSDDERLL YLGSALESLR GTFFRQAMFA
EFERDVHARV DKGESLTGAG LTKIYGDILR RYHGDKEGIV HIDDQVAIEW AYIPHFYNSF
YVFQYATSIA AGSLFADAIL KGEPGARERY LNVLKAGSSA YPYELVKAAG VDLATPAPYQ
AVVARMNRIM DEIETIVARR K
//
