ID C9RP58_FIBSS Unreviewed; 415 AA.
AC C9RP58;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Peptidase T {ECO:0000313|EMBL:ADL26486.1};
DE EC=3.4.11.14 {ECO:0000313|EMBL:ADL26486.1};
GN Name=pepT {ECO:0000313|EMBL:ADL26486.1};
GN OrderedLocusNames=FSU_1364 {ECO:0000313|EMBL:ADL26486.1};
OS Fibrobacter succinogenes (strain ATCC 19169 / S85).
OC Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC Fibrobacter.
OX NCBI_TaxID=59374 {ECO:0000313|EMBL:ADL26486.1, ECO:0000313|Proteomes:UP000000517};
RN [1] {ECO:0000313|Proteomes:UP000000517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19169 / S85 {ECO:0000313|Proteomes:UP000000517};
RA Durkin A.S., Nelson K.E., Morrison M., Forsberg C.W., Wilson D.B.,
RA Russell J.B., Cann I.K.O., Mackie R.I., White B.A.;
RT "Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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; CP002158; ADL26486.1; -; Genomic_DNA.
DR RefSeq; WP_014545661.1; NC_017448.1.
DR AlphaFoldDB; C9RP58; -.
DR STRING; 59374.FSU_1364; -.
DR MEROPS; M20.003; -.
DR GeneID; 34755266; -.
DR KEGG; fsc:FSU_1364; -.
DR PATRIC; fig|59374.8.peg.1313; -.
DR eggNOG; COG2195; Bacteria.
DR HOGENOM; CLU_053676_0_0_0; -.
DR OrthoDB; 9804934at2; -.
DR Proteomes; UP000000517; Chromosome.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0045148; F:tripeptide aminopeptidase activity; IEA:InterPro.
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 CDD; cd03892; M20_peptT; 1.
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; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:ADL26486.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADL26486.1};
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 Zinc {ECO:0000256|PIRSR:PIRSR037215-2}.
FT DOMAIN 216..317
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 80
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT ACT_SITE 184
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
SQ SEQUENCE 415 AA; 45782 MW; 7C0ECDDB8606AE9B CRC64;
MKVQDRFLKY VSFTTTSDEN SESCPSTKQQ LELAKFLTEE LEQIGLSQVK MDENGYVYGL
LPATEGRESD TPIGFISHMD TSPDFSGVNP KPQIIEDYDG EDVLLKGSGA VLKVEDFPTL
KWLKGRTLIT TDGTTLLGAD DKAGIAEIVT AMEELIEIDR HAESRGYENL SGHGDIWVCF
TPDEEIGRGA DRLDLSYFTA KYAYTVDGGY EGDIAYENFN AASATFKIHG KGVHPGEAKG
IMKNASLMAA EIAMALPENE TPATTEGREG FYHLTDMQGD VTEATLNYIV RDHDQTRFEE
RQEFLREIAK KFNEKFGEGS IELELKHSYS NMLQIIEKTP EVLERARTAI AAENITPVSD
PVRGGTDGAK LSFMGLPCPN LGTGGYGYHG PFEHVTVEGM ETVVRIIKRI ATSRG
//
