ID A0A1H0DL54_9BACL Unreviewed; 599 AA.
AC A0A1H0DL54;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=SAMN04487897_104154 {ECO:0000313|EMBL:SDN70788.1};
OS Paenibacillus sp. yr247.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1761880 {ECO:0000313|EMBL:SDN70788.1, ECO:0000313|Proteomes:UP000198936};
RN [1] {ECO:0000313|EMBL:SDN70788.1, ECO:0000313|Proteomes:UP000198936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR247 {ECO:0000313|EMBL:SDN70788.1,
RC ECO:0000313|Proteomes:UP000198936};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNIF01000004; SDN70788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0DL54; -.
DR STRING; 1761880.SAMN04487897_104154; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000198936; 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; cd09609; 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 InterPro; IPR034009; M3B_PepF_4.
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:SF45; SIMILAR TO OLIGOENDOPEPTIDASE; 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:UP000198936};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 114..183
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 209..585
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 599 AA; 67451 MW; E2F9DE7DFC1B5EFC CRC64;
MKQRLLRNEV PIELTWDLSE LFPSNQAWET ELKTLQELAT HIQQYKGNLQ NGASHLADCL
EAQEGLLERT MRVATYARLR FTEDTSNPQN QADSIRSGDA TSGIGAALSF IRSEILALPD
GTIEGYIKEE PRLEPFRKSL DDLLETKPHQ LSAETEAVLA SLSEVLGAPY NIYQRSKLSD
MSFSSVNDEQ GVTHPVSFAL FETDYEFSAN TTLRRASYES FTMTLEKYQN TFAATYATEV
KRQTVTANLR GYVSVTDMLL QPQQVTKEMY HTILDVIRME LAPHMQRLMK LKKKVLGLDR
LLFCDLKAPF DPEFNPSVTT QEAGSTILEA LNVMGPEYTE LMEQALSQRW IDYADNVGKS
TGAFCASPYG AHPFILITWA GNMRSAFTLA HELGHAGHLM LAARYQRYTN FRPSTYFIEA
PSTMNELLLA EHILKQSSDP RMKRWVILQL LNTYYHNFVT HLLEGDMQSR VYALAESGEA
LTAKKLSSLK GNVLSEFWGD AVELEPGANL TWMRQPHYYM GLYPYTYAAG LTASTAVVQL
MKEEGQPVID RWLEVLKAGG TVRPLDLLKH AGVDMADAKP IRSAVAYVGS LVDELERLF
//
