AMPT_THEAQ
ID AMPT_THEAQ Reviewed; 408 AA.
AC P23341;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Aminopeptidase T;
DE Short=AP-T;
DE EC=3.4.11.-;
DE AltName: Full=Heat-stable aminopeptidase;
OS Thermus aquaticus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 25104 / DSM 625 / JCM 10724 / NBRC 103206 / NCIMB 11243 / YT-1;
RX PubMed=1368580; DOI=10.1271/bbb1961.54.2385;
RA Motoshima H., Azuma N., Kaminogawa S., Ono M., Minagawa E., Matsuzawa H.,
RA Ohta T., Yamauchi K.;
RT "Molecular cloning and nucleotide sequence of the aminopeptidase T gene of
RT Thermus aquaticus YT-1 and its high-level expression in Escherichia coli.";
RL Agric. Biol. Chem. 54:2385-2392(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25104 / DSM 625 / JCM 10724 / NBRC 103206 / NCIMB 11243 / YT-1;
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 [3]
RP PROTEIN SEQUENCE OF 1-34.
RC STRAIN=ATCC 25104 / DSM 625 / JCM 10724 / NBRC 103206 / NCIMB 11243 / YT-1;
RA Minagawa E., Kaminogawa S., Matsuzawa H., Ohta T., Yamauchi K.;
RT "Isolation and characterization of a thermostable aminopeptidase
RT (aminopeptidase T) from Thermus aquaticus YT-1, an extremely thermophilic
RT bacterium.";
RL Agric. Biol. Chem. 52:1755-1759(1988).
CC -!- FUNCTION: Metal-dependent exopeptidase. {ECO:0000269|PubMed:1368580}.
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:1368580};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P42778};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P42778};
CC Note=Binds 2 divalent metal cations per subunit. Can use cobalt, zinc,
CC and possibly also magnesium ions. {ECO:0000250|UniProtKB:P42778};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1368580}.
CC -!- SIMILARITY: Belongs to the peptidase M29 family. {ECO:0000305}.
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DR EMBL; D00814; BAA00695.1; -; Genomic_DNA.
DR EMBL; D87664; BAA13426.1; -; Genomic_DNA.
DR PIR; JN0087; JN0087.
DR RefSeq; WP_053768123.1; NZ_LHCI01000106.1.
DR AlphaFoldDB; P23341; -.
DR SMR; P23341; -.
DR MEROPS; M29.001; -.
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; -; 1.
DR InterPro; IPR035097; M29_N-terminal.
DR InterPro; IPR000787; Peptidase_M29.
DR Pfam; PF02073; Peptidase_M29; 1.
DR PRINTS; PR00919; THERMOPTASE.
PE 1: Evidence at protein level;
KW Aminopeptidase; Cobalt; Direct protein sequencing; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Zinc.
FT CHAIN 1..408
FT /note="Aminopeptidase T"
FT /id="PRO_0000079175"
FT BINDING 250
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P42778"
FT BINDING 316
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P42778"
FT BINDING 316
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P42778"
FT BINDING 340
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P42778"
FT BINDING 340
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P42778"
FT BINDING 345
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P42778"
FT BINDING 376
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P42778"
FT BINDING 378
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P42778"
SQ SEQUENCE 408 AA; 44821 MW; 2BFC4EEFD60A63C3 CRC64;
MDAFTENLNK LAELAIRVGL NLEEGQEIVA TAPIEAVDFV RLLAEKAYEN GASLFTVLYG
DNLIARKRLA LVPEAHLDRA PAWLYEGMAK AFHEGAARLA VSGNDPKALE GLPPERVGRA
QQAQSRAYRP TLSAITEFVT NWTIVPFAHP GWAKAVFPGL PEEEAVQRLW QAIFQATRVD
QEDPVAAWEA HNRVLHAKVA FLNEKRFHAL HFQGPGTDLT VGLAEGHLWQ GGATPTKKGR
LCNPNLPTEE VFTAPHRERV EGVVRASRPL ALSGQLVEGL WARFEGGVAV EVGAEKGEEV
LKKLLDTDEG ARRLGEVALV PADNPIAKTG LVFFDTLFDE NAASHIAFGQ AYAENLEGRP
SGEEFRRRGG NESMVHVDWM IGSEEVDVDG LLEDGTRVPL MRRGRWVI
