ID D1VV72_9FIRM Unreviewed; 403 AA.
AC D1VV72;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=tripeptide aminopeptidase {ECO:0000256|ARBA:ARBA00012563};
DE EC=3.4.11.4 {ECO:0000256|ARBA:ARBA00012563};
GN Name=pepT {ECO:0000313|EMBL:EFA89569.1};
GN ORFNames=HMPREF0628_0099 {ECO:0000313|EMBL:EFA89569.1};
OS Peptoniphilus lacrimalis 315-B.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=596330 {ECO:0000313|EMBL:EFA89569.1, ECO:0000313|Proteomes:UP000005711};
RN [1] {ECO:0000313|EMBL:EFA89569.1, ECO:0000313|Proteomes:UP000005711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=315-B {ECO:0000313|EMBL:EFA89569.1,
RC ECO:0000313|Proteomes:UP000005711};
RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Strausberg R.L.,
RA Nelson K.E.;
RT "Genome Sequence of Peptoniphilus lacrimalis 315-B.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of the N-terminal residue from a tripeptide.;
CC EC=3.4.11.4; Evidence={ECO:0000256|ARBA:ARBA00000870};
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 -!- 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:EFA89569.1}.
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DR EMBL; ADDO01000062; EFA89569.1; -; Genomic_DNA.
DR RefSeq; WP_004825827.1; NZ_ADDO01000062.1.
DR AlphaFoldDB; D1VV72; -.
DR eggNOG; COG2195; Bacteria.
DR Proteomes; UP000005711; Unassembled WGS sequence.
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 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.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:EFA89569.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EFA89569.1};
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:UP000005711};
KW Zinc {ECO:0000256|PIRSR:PIRSR037215-2}.
FT DOMAIN 203..302
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 79
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT ACT_SITE 171
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 375
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
SQ SEQUENCE 403 AA; 45568 MW; D48CD97C4D6EB867 CRC64;
MEKLVERFLK YISFETTSDE SSDTCPSNPK EFELARYLEK EMKDLGLKDV YLSENCYLYA
TLPGTDKNKK TIGFISHMDT SPDMSGKNVN PRIIENYDGK DIKLNEEFVT SLKDFPFLKD
LKGHDIIVTD GTSLLGADDK AGIAIIMTAI ENLMKSNEKY GDIKIAFTPD EEIGRGADLF
DVERFAADFA YTVDGGAEGE FEYENFNAAS AKISIQGKNV HPGSAKNAMV NSILIAMELN
SLLPADQRPE HTEGREGFFH LNDFNGNVEY SQMYYIIRDH SFEKFEEKKK FLEEAVKFLN
IKYDNRIKLE IKDQYYNMKE KILPHMEIVD LALESMKKAG VKSEIIATRG GTDGSQLSYK
GLPCPNLFTG GYNYHGRYEL VSITTMKKTV KTVENIGKIG VEK
//
