ID A0A1I1Z2Z3_9FIRM Unreviewed; 595 AA.
AC A0A1I1Z2Z3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=SAMN02910278_00460 {ECO:0000313|EMBL:SFE26204.1};
OS Peptostreptococcus sp. D1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptostreptococcus.
OX NCBI_TaxID=72304 {ECO:0000313|EMBL:SFE26204.1, ECO:0000313|Proteomes:UP000199190};
RN [1] {ECO:0000313|EMBL:SFE26204.1, ECO:0000313|Proteomes:UP000199190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1 {ECO:0000313|EMBL:SFE26204.1,
RC ECO:0000313|Proteomes:UP000199190};
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; FONP01000001; SFE26204.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1Z2Z3; -.
DR STRING; 72304.SAMN02910278_00460; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000199190; 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:UP000199190};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 112..180
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 202..580
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 595 AA; 69951 MW; 2617E9A9ABD0CB59 CRC64;
MLKNREDIQL EYKWNLDDMY KDSEQINKDI EFIEGSFEIF ESYKGRLSES KEAFYEVLKL
MEDTSRVLSH YYVYTHMRHH EDTRINENQA VSTKSEMMST ELGKATAYIV PEIISMDEEL
LNEFLKDEKI SHYKKMIDEI LRDKPYTLSE KEEQIMAAVS ELTSTPENTY EMLTYADMEF
PEIMDEENEK VRLTHFNYST FIKSKDRRVR RDAFEAEFST YKKYSNTFAS TLFGGIKAEV
FNSRVRKFPS AIFASLYSDN ISVEVYNNLI ASIHDSIPVL DRYNNLRKEY FGLEEMHMYD
LYLPMARDFK IEISYKEAQS IILEALKPMG KYYISLIKRA FSERWIDVYE NEGKRGGAYS
WGSYDSHPYI LMSYKDDLNS LFTLIHELGH SIHSYLSREA QPYIYSGYKI FVAEVASTVN
ETLLIKYLLE KSNDIDEKVY LLNYYLEQYR TTVFRQTLFA EFEKIVHEKV EEGNPMTADD
FTKVYYELNQ LYYGNSCVVD ELVGIEWARI PHFYSNFYVY KYATGFSAAS VLSNKILQGG
ESVERYIEFL KSGGSEYPLD QLRKAGVDME KKEAVDSSLA IFSELVDELE KLVRD
//
