AMPT_GEOSE
ID AMPT_GEOSE Reviewed; 30 AA.
AC P00728;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Thermophilic aminopeptidase 1 alpha chain;
DE EC=3.4.11.-;
DE AltName: Full=Thermophilic aminopeptidase I alpha chain;
DE Flags: Fragment;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX PubMed=4521203; DOI=10.1073/pnas.70.12.3781;
RA Stoll E., Ericsson L.H., Zuber H.;
RT "The function of the two subunits of thermophilic aminopeptidase I.";
RL Proc. Natl. Acad. Sci. U.S.A. 70:3781-3784(1973).
CC -!- FUNCTION: Metalloenzyme of broad specificity, releasing all N-terminal
CC amino acids.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Binds 2 divalent metal cations per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Highly thermostable.;
CC -!- SUBUNIT: 12 chains of two different but homologous types, alpha and
CC beta, which can combine in various ratios.
CC -!- SIMILARITY: Belongs to the peptidase M42 family. {ECO:0000305}.
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DR PIR; A00908; AIBSAF.
DR AlphaFoldDB; P00728; -.
DR SMR; P00728; -.
DR PRIDE; P00728; -.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Aminopeptidase; Direct protein sequencing; Hydrolase; Metalloprotease;
KW Protease.
FT CHAIN 1..>30
FT /note="Thermophilic aminopeptidase 1 alpha chain"
FT /id="PRO_0000071652"
FT NON_TER 30
SQ SEQUENCE 30 AA; 3274 MW; D712C9C23E618142 CRC64;
AKLDETLTML KALTDAKGVP GNEREARDVM