ID W5ST46_BORAN Unreviewed; 589 AA.
AC W5ST46;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=BAN_0090400 {ECO:0000313|EMBL:AHH08211.1};
OS Borrelia anserina BA2.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borrelia.
OX NCBI_TaxID=1313293 {ECO:0000313|EMBL:AHH08211.1, ECO:0000313|Proteomes:UP000019262};
RN [1] {ECO:0000313|EMBL:AHH08211.1, ECO:0000313|Proteomes:UP000019262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA2 {ECO:0000313|EMBL:AHH08211.1,
RC ECO:0000313|Proteomes:UP000019262};
RA Schwan T.G., Raffel S.J., Porcella S.F., Martens C.A., Bruno D.P.,
RA Rickefs S.M., Barbian K.B.;
RT "Comparative Genomics of Relapsing Fever Spirochetes.";
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}.
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DR EMBL; CP005829; AHH08211.1; -; Genomic_DNA.
DR RefSeq; WP_025419454.1; NZ_CP005829.1.
DR AlphaFoldDB; W5ST46; -.
DR PATRIC; fig|1313293.3.peg.250; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_2_0_12; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000019262; Chromosome.
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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 113..178
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 194..575
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 589 AA; 69578 MW; 4118572CC0BD79B4 CRC64;
MTERSKINED DKWDLSSLFK NDEEYKATVK KIKSKLQDFK KYEKLEFNLN TFKQALNDYY
EIEEELEKTI YYTSIQLETD VSNKTANELR TINVNLETDA SNATSFFIPK IFKTDTQKIK
EWIKDKELKD KKIAIEKILR EKEHILSEDE EKILANYTSL YSSYNDIFSA LTNADMEFGE
IEGKPLSNST YSLFLQNENQ EIRREAFLKF YKEYKKHENT LANLLISDIN KNKFLAKTRK
FKDTISMKLF QNNIDKKVYT NLIETVNENL SVLHEYYEFR KNTLNQEYLN HYDIYVPLTK
DIKFKHSFKE ACNKILKSLE ILGSEYTEVL KKGLLEERWV DKYENKGKRA GAFSAGSYNG
KPYILMNYKD ESIRDMFTLA HEAGHSMHSY FSIKNNPFPQ YKYSIFEAEI ASTVNEQILA
DYLLKNENDI EKIKYIKINQ IDDLLATFFR QTMFAEFEYI IHEMINKDEP VIKETIKTTY
LKLLKKYFGP SLKFDENSSL ECFRVPHFYS SFYVYQYATG ITAALLIYKN IKDNKKDATK
NYMEFLKTGG SKYPLESLKV TGVNLSLKST IQNTINIFKE RLDDVKQLF
//