ID G8QQ54_SPHPG Unreviewed; 596 AA.
AC G8QQ54;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN OrderedLocusNames=SpiGrapes_0802 {ECO:0000313|EMBL:AEV28631.1};
OS Sphaerochaeta pleomorpha (strain ATCC BAA-1885 / DSM 22778 / Grapes).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Sphaerochaetaceae;
OC Sphaerochaeta.
OX NCBI_TaxID=158190 {ECO:0000313|EMBL:AEV28631.1, ECO:0000313|Proteomes:UP000005632};
RN [1] {ECO:0000313|EMBL:AEV28631.1, ECO:0000313|Proteomes:UP000005632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1885 / DSM 22778 / Grapes
RC {ECO:0000313|Proteomes:UP000005632};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Munk A.C., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Ritalahtilisa K.,
RA Loeffler F., Woyke T.;
RT "Complete sequence of Spirochaeta sp. grapes.";
RL Submitted (NOV-2011) 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; CP003155; AEV28631.1; -; Genomic_DNA.
DR RefSeq; WP_014269480.1; NC_016633.1.
DR AlphaFoldDB; G8QQ54; -.
DR STRING; 158190.SpiGrapes_0802; -.
DR KEGG; sgp:SpiGrapes_0802; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_2_0_12; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000005632; 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: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:UP000005632};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 113..181
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 201..582
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 596 AA; 68439 MW; DE1EFA42D5001736 CRC64;
MHIATRSEVN ETDTWDLSAL FPSAKEWEKG MEELKNRIEE APLFKGQLIA GKESFLKVLS
WYKETGILAE SLANWAFLNY SADASDNMNV QRYSMVTQEL ARLGTNMAYF DPELLLIEES
VINTYLDDPD FSQYKVYLKK SRRFKQYILS EKEERLMALE SEVGATAKTT FQDLTNVDFD
FGMIETKEGL KPLTQSTFSS FMMQEDRELR KKVYLQFYKN YESHKMTIAR LYEGQVKQDM
FRCKARGYDS CRQKALFPDN VPQKVYDNLI SCVHEALPSL HRYYALRAKL MGLESLAHYD
VYVPLVSGVQ TKTSYDEAVD IVCKALAPLG EEYVTVIENG LTSERWVDRY ENKGKRSGAF
SSGCYSGKPY ILLNYKEDVL RDLFTIAHEG GHSMHSFYSV RNNPYFQYDY TIFEAEVAST
FNEQLVANYL LETAKDTKTK AFILSKQLDD IVATLYRQTM FAEYEDTTHR LAEGGTPLTV
ETLRSEYGKL LKAYFGPMVT FEEQSDLEGL RIPHFYSSFY VYKYATGISA AIALSQKVLN
GGEKERQDYL AFLKSGGSEF PIDSLKKAGV DMEQAEPIRS ALKYFASLLD EFEKLL
//