ID A0A061AG65_9MOLU Unreviewed; 405 AA.
AC A0A061AG65;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Tripeptide aminopeptidase/Peptidase T {ECO:0000313|EMBL:CDR30561.1};
GN Name=pepT {ECO:0000313|EMBL:CDR30561.1};
GN ORFNames=Aocu_04880 {ECO:0000313|EMBL:CDR30561.1};
OS Acholeplasma oculi.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Acholeplasma.
OX NCBI_TaxID=35623 {ECO:0000313|EMBL:CDR30561.1, ECO:0000313|Proteomes:UP000032434};
RN [1] {ECO:0000313|Proteomes:UP000032434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kube M.;
RL Submitted (MAY-2014) 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}.
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DR EMBL; LK028559; CDR30561.1; -; Genomic_DNA.
DR RefSeq; WP_045749097.1; NZ_UFRU01000001.1.
DR AlphaFoldDB; A0A061AG65; -.
DR STRING; 35623.Aocu_04880; -.
DR MEROPS; M20.003; -.
DR KEGG; aoc:Aocu_04880; -.
DR PATRIC; fig|35623.3.peg.489; -.
DR HOGENOM; CLU_053676_0_0_14; -.
DR InParanoid; A0A061AG65; -.
DR OrthoDB; 9804934at2; -.
DR Proteomes; UP000032434; 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.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:CDR30561.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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:UP000032434};
KW Zinc {ECO:0000256|PIRSR:PIRSR037215-2}.
FT DOMAIN 204..298
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 172
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 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
SQ SEQUENCE 405 AA; 45606 MW; 44A54AA2F5D48714 CRC64;
MNRLVERFLR YVKIDTQSDP DSTTFPSTLK QLDLSKMLVE ELKGMGLDAF LDKDGYVYSK
LPSNIKKDVP SIGFIAHVDT SFDAPGQGVN PRIIKNYQGE HIQLDETYHM EPKQYPSLKK
VIGEDIIVTD GKTLLGADDK AGVAEIMEMV ERLVEDPSIE HGDIYICFTP DEEIGKGADR
FNYEWFKADF AYTADGSEVG GIEYENFNAA SAKVKFTGKS IHPGASKNKM INALHLQMKF
HQMLPTFMNP AFTEGYEGFN HLTEVKGHVE EATAKYIIRN HDMSIFNGQK EKFIQIAKYM
NDSYGYECVS VELNDSYYNM YEVIKDHMYV IDYAVAATKK SGLTPKFEAI RGGTDGARLT
FGGLICPNLG TGAYHFHGRL EFASIQQMEK AVEVFTNIVK EVTLK
//
