ID A0A1X7H2A5_9BACL Unreviewed; 596 AA.
AC A0A1X7H2A5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=SAMN05661091_1552 {ECO:0000313|EMBL:SMF78368.1};
OS Paenibacillus uliginis N3/975.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1313296 {ECO:0000313|EMBL:SMF78368.1, ECO:0000313|Proteomes:UP000192940};
RN [1] {ECO:0000313|EMBL:SMF78368.1, ECO:0000313|Proteomes:UP000192940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N3/975 {ECO:0000313|EMBL:SMF78368.1,
RC ECO:0000313|Proteomes:UP000192940};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; LT840184; SMF78368.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7H2A5; -.
DR STRING; 1313296.SAMN05661091_1552; -.
DR Proteomes; UP000192940; Chromosome i.
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:UP000192940};
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 202..582
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 596 AA; 68602 MW; 9E5D008C3C5A1153 CRC64;
MEKVMKRSEV PTEHQWKLQD LFTDQKAWDN AYNEVQRLIK TAADFQGKLT NAESIKQCFD
LEDEVGLHTE RLFVYAHMHH DEDTANPTYQ ALTQKAKKLS VEVGEALSFT TPEILALSEG
ELDKLIADPT LADYRFTLTE MKREKAHILS KAEEALLAQV GNMSSAPQTI FGMLNNADMK
FPKIKDENGK EVELTHGSYI QFLENPNREV REAAFKAVYE TYGKQKNTIS ATLSANVNKN
IFYSRVRKYP SVLEMSLYGD NIPKEVYTNL IDTIHESLPL LHRYMNLRKK LLGVDELHMY
DLFAPLVEEY KMDITYDQAK QTIKDGLHPL GEDYLKNLQD GYDNGWIDVY ENENKRTGAY
SWGAYGTHPY VLLNHKDNLN SMFTLAHEMG HALHSFYSDT NLKYRDAQYT IFLAEVASTT
NEALLMDYLL KKSTDPKEKM YLLTYYADQF RTTVFRQTMF AEFEKIVHER AESGESLTPQ
DLSDIYYDLN VKYHGKNMTV DKEIGMEWAR IPHFYNSFYV YKYATGFSAA TSFSKQILEE
GQPAVDRYLG FLKSGGSDFS INILKKAGVD MSSPEPIREA MSVFENVISQ MEELTK
//