ID K9EAU1_9LACT Unreviewed; 604 AA.
AC K9EAU1;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=HMPREF9698_00072 {ECO:0000313|EMBL:EKU94344.1};
OS Alloiococcus otitis ATCC 51267.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Alloiococcus.
OX NCBI_TaxID=883081 {ECO:0000313|EMBL:EKU94344.1, ECO:0000313|Proteomes:UP000009875};
RN [1] {ECO:0000313|EMBL:EKU94344.1, ECO:0000313|Proteomes:UP000009875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51267 {ECO:0000313|EMBL:EKU94344.1,
RC ECO:0000313|Proteomes:UP000009875};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Alloiococcus otitis ATCC 51267.";
RL Submitted (SEP-2012) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKU94344.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGXA01000002; EKU94344.1; -; Genomic_DNA.
DR RefSeq; WP_003776179.1; NZ_JH992957.1.
DR AlphaFoldDB; K9EAU1; -.
DR STRING; 883081.HMPREF9698_00072; -.
DR MEROPS; M03.007; -.
DR PATRIC; fig|883081.3.peg.72; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_2_0_9; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000009875; 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:UP000009875};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 116..185
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 206..586
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 604 AA; 69109 MW; B15675F4131F36D3 CRC64;
MSQNELPSRQ EVDPKLTWDL TPIFASDQAW EEAFEEVKDQ IKEVAQYQGT LDQGPKAFQQ
ALEANLDLSR KLESVYVYSH LKHDQDTSNG DYQALEDRAR GLLAQAATAT AWFQPELLAL
EEGKVASYLD QNPDLEVYRH ELNQQLAKKD HVLDADKEGL LAGASEIFSS GSQTFNILNN
ADLTFPLVQN EEGDQVRLSH GLYGQLLEST DRNVRRQAFE KLYEVYQSFN NTLASTLQTE
VKKNNYLARV HNYNSARHQA LSNNNIPESV HETLIEVVND NLPLFHRYLA LRKKVLGLDE
LHMYDLYTPI AGESSLKYTF EEAREETYKS LAKLGPDYKA VLDRAFQDRW IDVVENKGKR
SGAYSSGGYD TNPYVLLNWH DSLDNLYTLV HELGHSVHSY FTRNSQPYIY GDYPIFLAEI
ASTTNENLLT HYLLENAQDP LTRVHVLNHY LDGFKGTVFR QTQFAEFEHH IHQAAAEGQP
LTGHYLNQTY GELNDRYYGD SVVNDDQIFF EWSRIPHFYM NYYVYQYSTG FCAATALADK
LVKEEDGALG AYLGYLKSGD SDYPIEIMKK AGVDMTNKAY IERAMKVFEE RLGQLEDALA
ELKD
//
