ID A0A1S8LR27_9CLOT Unreviewed; 588 AA.
AC A0A1S8LR27;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Oligoendopeptidase F, plasmid {ECO:0000313|EMBL:OOL84454.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:OOL84454.1};
GN Name=pepF1 {ECO:0000313|EMBL:OOL84454.1};
GN ORFNames=CROST_013290 {ECO:0000313|EMBL:URZ10619.1}, CROST_44250
GN {ECO:0000313|EMBL:OOL84454.1};
OS Clostridium felsineum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=36839 {ECO:0000313|EMBL:OOL84454.1};
RN [1] {ECO:0000313|EMBL:OOL84454.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7320 {ECO:0000313|EMBL:OOL84454.1};
RA Poehlein A., Montoya Solano J.D., Flitsch S., Krabben P., Duerre P.,
RA Daniel R.;
RT "Microbial solvent formation.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:URZ10619.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 7320 {ECO:0000313|EMBL:URZ10619.1};
RA Poehlein A., Schoch T., Duerre P., Daniel R.;
RT "Genome sequence of C. roseum typestrain.";
RL Submitted (APR-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|RuleBase:RU003435}.
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DR EMBL; LZYV01000104; OOL84454.1; -; Genomic_DNA.
DR EMBL; CP096983; URZ10619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8LR27; -.
DR STRING; 84029.CROST_44250; -.
DR KEGG; crw:CROST_013290; -.
DR Proteomes; UP000190951; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09607; 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; IPR034006; M3B_PepF_2.
DR InterPro; IPR042088; OligoPept_F_C.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU003435, ECO:0000313|EMBL:OOL84454.1};
KW Metal-binding {ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|RuleBase:RU003435};
KW Zinc {ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 194..574
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 588 AA; 68585 MW; 8F1BC81EE3712452 CRC64;
MDLTWNLDNI YTSFESEKFK EDSREFEKIT ARINNFNFNM LEKDITKLKI EDFLKCISEY
QRLYYKIYSY AYLIISANTE NIKAMQVLDD IENKKLESNK SFVKFSKCLY KFNDLDEIIN
GSMYLLEHKV YLKELVLKAK YLLDGREEFI INKMQSTGAR NLERLYMETV GSEVEEISVD
GKNDKFTLPE LHEMLYSKDA VTRKKAYYKE IDLCRNLARV SASCINGISG EAINVCSLRD
FNSPLEKVLM KSRMNVKTLE VMMEAIKESL PIFQKYFAKK AKVLGYKSNL PFYDIYAPIS
DSDIKVSYDE AESLIISSFK NFSSKLSDFA GKVFKNRWID AEPRKGKVNF GLSICVFPIK
ESRIIVNFNE SYNDVSILAH EIGHAYHDSK LYSKSILNTE YPVPMAETAS IFCETILSNE
LVNKLPKKEA VDILEKDISN TAYFIVDFYG RYLFEKELYE RRRSGILTIE ELNEMMFKCM
KKSYGKAIDQ KTIHPYMWLN KAGYFMPENE FLNFPYSFGV LFSKGLYAKY VSNKKSFAEK
YDKFLEQTSS MNMVDAAKLL EVDINSIEFF RASIKLIEKD IEKFIELA
//
