ID A0A1I5VJZ0_9BACI Unreviewed; 604 AA.
AC A0A1I5VJZ0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=SAMN05421670_0853 {ECO:0000313|EMBL:SFQ07783.1};
OS Psychrobacillus psychrotolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX NCBI_TaxID=126156 {ECO:0000313|EMBL:SFQ07783.1, ECO:0000313|Proteomes:UP000198734};
RN [1] {ECO:0000313|Proteomes:UP000198734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11706 {ECO:0000313|Proteomes:UP000198734};
RA Varghese N., Submissions S.;
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; FOXU01000001; SFQ07783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5VJZ0; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000198734; 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:UP000198734};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 115..181
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 207..583
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 604 AA; 69257 MW; AD43EAE322EBF517 CRC64;
MVNHMPKRDE VKTEETWNLN DLFQTENDFS GALKEIEQNA LEFNNRYHGN IQNATDVVDA
LIEYTKLYEK IVPAGAFASL SLSTDQTNTD AQMRASKFGS LSAKVSSQLS FLNSELVELP
EAIIKEAISK SPAHQIYLDK LLAKKKYQLH PEVEKTLAAF SASFGAPYKL YDTTKMLDIA
FDNFEVNGQE YPLSYVSFEN DWEGEADTEK RRAAFESFSK KLKEYQHTTA KTYDMHLQME
KTTSDLRGYD SVYDYLLFNQ DVDRSLYNRQ IDLITKELAP HMRKYAKLLQ KEHGLEKMTF
ADLKISLDPT YEPKISVEES KNYIDDALSV MGEEYIEMVN RAYVERWIDF PQNAGKSTGA
FCSSPYGSHP YILISWSSRM NEVFVLAHEL GHAGHFYYAN KEQNIFNARP SLYFIEAPST
MNEMLVANHL LKNSDDPKFK RWVISSIVAR TYYHNFVTHL LEAAYQRKVY DRIDQGLNVN
AQILNDYKRS VLEEFWGDAV EITEGAELTW MRQPHYYMGL YPYTYSAGLT ISTQVSKRIL
EEGQTAVDEW TEVLKAGGTK SPVELAQMAG VDITTDKPLK DTIAYIGSLI DELESLTEEI
NQNN
//
