ID A0A2M8MUJ9_9RHOB Unreviewed; 421 AA.
AC A0A2M8MUJ9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Peptidase T {ECO:0000313|EMBL:PJF07882.1};
GN Name=pepT {ECO:0000313|EMBL:PJF07882.1};
GN ORFNames=CUR21_16840 {ECO:0000313|EMBL:PJF07882.1};
OS Pseudorhodobacter sp. MZDSW-24AT.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudorhodobacter.
OX NCBI_TaxID=2052957 {ECO:0000313|EMBL:PJF07882.1, ECO:0000313|Proteomes:UP000230388};
RN [1] {ECO:0000313|EMBL:PJF07882.1, ECO:0000313|Proteomes:UP000230388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MZDSW-24AT {ECO:0000313|EMBL:PJF07882.1,
RC ECO:0000313|Proteomes:UP000230388};
RA Mayilraj S.;
RT "Pseudorhodobacter sp. nov., strain MZDSW-24AT genome sequence and
RT assembly.";
RL Submitted (NOV-2017) 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 -!- 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:PJF07882.1}.
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DR EMBL; PGOI01000013; PJF07882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8MUJ9; -.
DR OrthoDB; 9804934at2; -.
DR Proteomes; UP000230388; Unassembled WGS sequence.
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 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:UP000230388};
KW Zinc {ECO:0000256|PIRSR:PIRSR037215-2}.
FT DOMAIN 210..286
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 82
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
SQ SEQUENCE 421 AA; 44610 MW; 3C6369CBBD050977 CRC64;
MTPFDAELEA RLTRYAALDS QSDAASPSAP STQVQWGILR LLADELTQIG AAEVRVTDYG
TVLATIPGTA PGPTIGFLAH VDTAPQFNAT GVKPRVIHGY NGGDITFPDA PGLILSPAAF
PYLASKQGHT IITASGTTLL GADDKAGVAI IMTAARHLLE TPQIPHGPIR IAFTPDEEIG
RGVDKRLPAD LAADFAYTFD GGAVGEVEYE SFSADGAVVK ITGVSIHPGT AYGRMVNAIP
LAAKIIAALP QSTMTPETTQ DREGFIHATD MTGGAAEMTL HFILRDFERD GLAQKGEILR
HVCAAVQATE PRAQITCTIT PQYRNMRYWL ENDMTPVTLA RAACARIGVA PVSVPIRGGT
DGSRLTEMGI PCPNLFTGMQ NIHGPLEWVS VQDMAKATEL FLALVQEAAS EDSRPAGRAA
R
//
