ID AMPT_THET8 Reviewed; 408 AA.
AC P42778; Q5SJ62;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Aminopeptidase T;
DE Short=AP-T;
DE EC=3.4.11.-;
DE AltName: Full=Heat-stable aminopeptidase;
GN OrderedLocusNames=TTHA1152;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9362117; DOI=10.1271/bbb.61.1710;
RA Motoshima H., Minagawa E., Tsukasaki F., Kaminogawa S.;
RT "Cloning of genes of the aminopeptidase T family from Thermus thermophilus
RT HB8 and Bacillus stearothermophilus NCIB8924: apparent similarity to the
RT leucyl aminopeptidase family.";
RL Biosci. Biotechnol. Biochem. 61:1710-1717(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) IN COMPLEX WITH ZINC IONS, CATALYTIC
RP ACTIVITY, FUNCTION, COFACTOR, AND SUBUNIT.
RX PubMed=16242715; DOI=10.1016/j.jmb.2005.09.042;
RA Odintsov S.G., Sabala I., Bourenkov G., Rybin V., Bochtler M.;
RT "Substrate access to the active sites in aminopeptidase T, a representative
RT of a new metallopeptidase clan.";
RL J. Mol. Biol. 354:403-412(2005).
CC -!- FUNCTION: Metal-dependent exopeptidase. {ECO:0000269|PubMed:16242715}.
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:16242715};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16242715};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16242715};
CC Note=Binds 2 divalent metal cations per subunit. Can use cobalt, zinc,
CC and possibly also magnesium ions. {ECO:0000269|PubMed:16242715};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16242715}.
CC -!- SIMILARITY: Belongs to the peptidase M29 family. {ECO:0000305}.
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DR EMBL; D13386; BAA02654.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70975.1; -; Genomic_DNA.
DR RefSeq; WP_011173220.1; NC_006461.1.
DR RefSeq; YP_144418.1; NC_006461.1.
DR PDB; 2AYI; X-ray; 3.70 A; A/B/C/D/E=1-408.
DR PDBsum; 2AYI; -.
DR AlphaFoldDB; P42778; -.
DR SMR; P42778; -.
DR MEROPS; M29.001; -.
DR EnsemblBacteria; BAD70975; BAD70975; BAD70975.
DR GeneID; 3170035; -.
DR KEGG; ttj:TTHA1152; -.
DR PATRIC; fig|300852.9.peg.1132; -.
DR eggNOG; COG2309; Bacteria.
DR HOGENOM; CLU_054346_1_0_0; -.
DR PhylomeDB; P42778; -.
DR EvolutionaryTrace; P42778; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1830.10; Thermophilic metalloprotease (M29); 1.
DR InterPro; IPR035097; M29_N-terminal.
DR InterPro; IPR000787; Peptidase_M29.
DR PANTHER; PTHR34448; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR34448:SF3; AMINOPEPTIDASE AMPS; 1.
DR Pfam; PF02073; Peptidase_M29; 1.
DR PRINTS; PR00919; THERMOPTASE.
DR SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Cobalt; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Zinc.
FT CHAIN 1..408
FT /note="Aminopeptidase T"
FT /id="PRO_0000079176"
FT BINDING 250
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:16242715"
FT BINDING 316
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:16242715"
FT BINDING 316
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:16242715"
FT BINDING 340
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:16242715"
FT BINDING 340
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:16242715"
FT BINDING 345
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:16242715"
FT BINDING 376
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:16242715"
FT BINDING 378
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:16242715"
SQ SEQUENCE 408 AA; 45018 MW; CBA7F8E0DA99A2D2 CRC64;
MDAFKRNLEK LAELAIRVGL NLEKGQEVIA TAPIEAVDFV RLLAEKAYRE GASLFTVIYG
DQELARKRLA LAPEEGLDKA PAWLYEGMAR AFREGAARLA VSGSDPKALE GLPPEKVGRA
QKANARAYKP ALEAITEFVT NWTIVPFAHP GWARAVFPGL PEEEAVRRLW EAIFQATRAD
QEDPIAAWEA HNRALHEKVA YLNARRFHAL HFKGPGTDLV VGLAEGHLWQ GGATATKGGR
LCNPNLPTEE VFTAPHRERV EGVVRASRPL ALGGTLVEGI FARFERGFAV EVRAEKGEEV
LRRLLDTDEG ARRLGEVALV PADNPIAKTG LVFFDTLFDE NAASHIAFGQ AYQENLEGRP
SGEAFRKRGG NESLVHVDWM IGSEEMDVDG LYEDGTRTPL MRRGRWVV
//
