ID A0A1I3ARN5_9LACT Unreviewed; 605 AA.
AC A0A1I3ARN5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=SAMN04489868_101142 {ECO:0000313|EMBL:SFH52399.1};
OS Pisciglobus halotolerans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae.
OX NCBI_TaxID=745365 {ECO:0000313|EMBL:SFH52399.1, ECO:0000313|Proteomes:UP000198668};
RN [1] {ECO:0000313|EMBL:SFH52399.1, ECO:0000313|Proteomes:UP000198668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27630 {ECO:0000313|EMBL:SFH52399.1,
RC ECO:0000313|Proteomes:UP000198668};
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; FOQE01000001; SFH52399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3ARN5; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000198668; 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:UP000198668};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 116..182
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 203..584
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 605 AA; 68533 MW; 199E6C652800FAD7 CRC64;
MSKEEMKTRA EVPVEQTWDT SALYETKAAF DQAVEELKKS VTKLATDYEG KLTDAETIIS
ALKDYGHIEK MASWTYHYAF LPESTDITNA ENVELSRSMS NLLAEIGSKT TFFAAELKAA
SDDVLDEVVA KAPQYASFIR HIKKDKKIQL ELPVEKALAR LSPVLNAPEN IYEQARLADM
DFGTFEAEGK VYPLSFVLYE DYYAYHPNTA IRRAAFDKFS NALAQYQNVV AAAYYTQVQK
EKTIATMRGF DSIFDYLLYD QEVDRAMYDR QIDTIMSELA PVMQKYITHL KEENSLDKMT
YADVKIDLDA AYSPEVTIEA SKGYVEEAIA ILGQDYVARV MKAYPERWVD FAQNKGKSTG
GFCTSPYGTH PYVLMSWTGQ LSDVYTLIHE FGHAAQGLLA AENNDILGVE PSLYLIEAPS
TFNELLLTHS LQQKATNARL ERYALAKMIT NTYFHNFITH LLEAAYQREV YQLVDEGKGF
DAAKLNELKR NVLKQFWGDA VEINPGAELT WMRQVHYYMG LYSYTYSAGL TIATQAFLRI
KEEGAPAVED WLTFLKTGDQ FEPAEAAKVA GVDITTDKPL KDTIHFLDES VDRIIELTQE
LKDVE
//
