ID A0A1N6GEE6_9LACT Unreviewed; 605 AA.
AC A0A1N6GEE6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=SAMN05878443_1172 {ECO:0000313|EMBL:SIO05856.1};
OS Carnobacterium alterfunditum.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=28230 {ECO:0000313|EMBL:SIO05856.1, ECO:0000313|Proteomes:UP000184758};
RN [1] {ECO:0000313|EMBL:SIO05856.1, ECO:0000313|Proteomes:UP000184758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=313 {ECO:0000313|EMBL:SIO05856.1,
RC ECO:0000313|Proteomes:UP000184758};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FSRN01000001; SIO05856.1; -; Genomic_DNA.
DR RefSeq; WP_034548111.1; NZ_FSRN01000001.1.
DR AlphaFoldDB; A0A1N6GEE6; -.
DR STRING; 28230.SAMN05878443_1172; -.
DR eggNOG; COG1164; Bacteria.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000184758; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 117..186
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 207..587
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 605 AA; 69655 MW; 4A3F3BFC3F4F8B45 CRC64;
MSEPKKLPKR DKIPDESTWD LGVIFQSDEA FKQSYKELEK KIESVVTYKG TLTNGSESFL
RAIQTILDLS NQMEKLYVYG QLKNDQDTTN SIYQGMYEQV TKLATQAHEA ISWFEPEVLE
LPEERLNHYF IENEELTIYK HFIDQLTATR EHVLSANEEA LLAGAGEIFN ASSRTFNILN
NADITFPTIK DENGDDIQLT HGVYGQLMES TDRSVRESAF KNLYKVYKGL QNTFSSTLSS
HVKYHNYNAK VHHYQSAREK ALSSNHIPES VYDTLLDVVH DHLPLLHRYV ALRKELLGVD
ELHMYDMYTP ISGEAGIKYT YEEAEAETLK ALQPLGEEYL SVLKKAFNNR WIDVIENEGK
RSGAYSSGAY ETNPYILLNW HDSLNHLYTL VHELGHSAHS YYTRTNQPYV YGDYSIFLAE
IASTTNENIL TDHLLETQTD PKVRAYVLNH YLDGFKGTMF RQTQFAEFEH FIHEEAAKGT
PLTSDFLTDY YGELNAQYYG PDVEKDPEIA IEWTRIPHFY YNYYVYQYST GFSAATALAD
KIVKGEEGAL DKYLTYLKSG NSDYPIEVMK KAGVDMTNKT YIEDAMKVFE ARLNELEELI
ETLKS
//
