ID E1QYT8_OLSUV Unreviewed; 449 AA.
AC E1QYT8;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Peptidase T {ECO:0000313|EMBL:ADK67552.1};
DE EC=3.4.11.4 {ECO:0000313|EMBL:ADK67552.1};
GN OrderedLocusNames=Olsu_0431 {ECO:0000313|EMBL:ADK67552.1};
OS Olsenella uli (strain ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 /
OS NCIMB 702895 / VPI D76D-27C) (Lactobacillus uli).
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Olsenella.
OX NCBI_TaxID=633147 {ECO:0000313|EMBL:ADK67552.1, ECO:0000313|Proteomes:UP000000333};
RN [1] {ECO:0000313|EMBL:ADK67552.1, ECO:0000313|Proteomes:UP000000333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 / NCIMB 702895 /
RC VPI D76D-27C {ECO:0000313|Proteomes:UP000000333};
RX PubMed=21304694; DOI=10.4056/sigs.1082860;
RA Goker M., Held B., Lucas S., Nolan M., Yasawong M., Glavina Del Rio T.,
RA Tice H., Cheng J.F., Bruce D., Detter J.C., Tapia R., Han C., Goodwin L.,
RA Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Rohde M., Sikorski J., Pukall R., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Olsenella uli type strain (VPI D76D-27C).";
RL Stand. Genomic Sci. 3:76-84(2010).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR037215-2};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR037215-
CC 2};
CC -!- SIMILARITY: Belongs to the peptidase M20B family.
CC {ECO:0000256|ARBA:ARBA00009692}.
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DR EMBL; CP002106; ADK67552.1; -; Genomic_DNA.
DR RefSeq; WP_013251304.1; NZ_JQCO01000001.1.
DR AlphaFoldDB; E1QYT8; -.
DR STRING; 633147.Olsu_0431; -.
DR GeneID; 78511881; -.
DR KEGG; ols:Olsu_0431; -.
DR PATRIC; fig|633147.7.peg.1127; -.
DR eggNOG; COG2195; Bacteria.
DR HOGENOM; CLU_053676_0_0_11; -.
DR OrthoDB; 9804934at2; -.
DR Proteomes; UP000000333; Chromosome.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0045148; F:tripeptide aminopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006518; P:peptide metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR010161; Peptidase_M20B.
DR NCBIfam; TIGR01882; peptidase-T; 1.
DR PANTHER; PTHR42994; PEPTIDASE T; 1.
DR PANTHER; PTHR42994:SF1; PEPTIDASE T; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037215; Peptidase_M20B; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:ADK67552.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADK67552.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037215-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000333};
KW Zinc {ECO:0000256|PIRSR:PIRSR037215-2}.
FT DOMAIN 246..346
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 118
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT ACT_SITE 214
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
SQ SEQUENCE 449 AA; 48437 MW; 80B5A39F4B22D13D CRC64;
MASATEHREP KHREPRPCEP RPCEPRPCEP RSYEPKPSDV LERFLRYVQV DSQSDPDNES
ETPSTPAQHD MARVLGEELR ALGCEDVVVD GHAYVTATVP ASAGAEGLPA LGLCAHIDST
VDAPAAGVRP HVVHYEGGDL VAGVIDGTEV STSSDQVPDL GQFVGQDIVV SDGRTLLSAD
DKAGVAEICA LVARLGDDPS LPHPTLKIAF VPDEEIGHGA ALLDLDKFGA AWCYTVDGEA
LGEFNYETFN AAEATVRVRG VMVHPGSAKD VMVNAITVAG EFERLVPAFE RPEHTEGREG
FYHPIQVRGT ASEVTLTYIV RDHDASRFEG RQQVLRDIAA FLNGRHGEGT VTVELREQYR
NMSEAFGDCP FLIANALEAH REVGIEPKVV AVRGGTDGSQ LSLRGLPCPN IATGGYNAHS
VREFVPVRSL ELTVDLLERL VGKFSVPQS
//
