ID A0A0M2WTL5_9BURK Unreviewed; 622 AA.
AC A0A0M2WTL5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN Name=pepF1 {ECO:0000313|EMBL:KKO66189.1};
GN ORFNames=VM94_00530 {ECO:0000313|EMBL:KKO66189.1};
OS Janthinobacterium sp. KBS0711.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=1649647 {ECO:0000313|EMBL:KKO66189.1, ECO:0000313|Proteomes:UP000034315};
RN [1] {ECO:0000313|EMBL:KKO66189.1, ECO:0000313|Proteomes:UP000034315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS0711 {ECO:0000313|EMBL:KKO66189.1,
RC ECO:0000313|Proteomes:UP000034315};
RA Shoemaker W.R., Muscarella M.E., Lennon J.T.;
RT "Genome sequence of the soil bacterium Jantinobacterium sp. KBS0711.";
RL Submitted (APR-2015) 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:KKO66189.1}.
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DR EMBL; LBCO01000004; KKO66189.1; -; Genomic_DNA.
DR RefSeq; WP_046682031.1; NZ_VCCE02000001.1.
DR AlphaFoldDB; A0A0M2WTL5; -.
DR PATRIC; fig|1649647.5.peg.543; -.
DR Proteomes; UP000034315; 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:UP000034315};
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..622
FT /note="Oligoendopeptidase F"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005646382"
FT DOMAIN 131..198
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 223..601
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 622 AA; 68792 MW; 1083A7100814D614 CRC64;
MTPSALKRPL LFSLLAFSLA TASAAPAPSD RQADRWDLTA LYQNDAAFDA DAKKLSAQLQ
QLGACKGQLG ARLKSCLDLY AEARKRVNTL TTYAAQYYDQ DTGDSKGNQL NQRAALLGND
FSQATTFLQP EILALGSKRI DAMLAKDKGL QLYRFQLSNM LRSAPHTLDA AGEQLVAQFG
LATGSAASVY RTLANAEIPW PTVKLSDGKE VRLDQAAYTK YRDDDNRADR KLVFDAFFGK
WKEYERTFGE TLYGQLKTDA AYAKVRRYAD SQSAALDADN LPPAVYQTLI AQTNANLPTL
HRYFKLRARM LGIKDLAYYD IYAPLLKSDR SFPLAEGKQM MLDSAAPLGP DYVKSLTAAV
DARWMDVYPR PRKVAGAYMN GDAYDVHPFV LLNYTDNYEA VSTLTHEWGH AMHSVLANKA
QPSIYAPYSI FVAEIASTTN EALLLDARLK QAKDDDERLL YLGAALENLR GTFFRQAMFA
EFEAAIHGKV DKGESLTGEE ITAIYAGILK RYHGEAQGVM SIDPAYALEW AYVPHFYHGY
YVFQYATSIA AAQDFAQRIL DKEPGALAAY LKMLGAGGSA YPYELVKAAG VDLASPKPYQ
ALVARMNGIM DQIEAIESRR GK
//
