AMPG_STRLI
ID AMPG_STRLI Reviewed; 73 AA.
AC Q54340;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Aminopeptidase G;
DE EC=3.4.11.-;
DE Flags: Fragment;
GN Name=pepG;
OS Streptomyces lividans.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1916;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=66 / 1326;
RX PubMed=7765336; DOI=10.1007/bf01569658;
RA Butler M.J., Aphale J.S., Dizonno M.A., Krygsman P., Walczyk E.,
RA Malek L.T.;
RT "Intracellular aminopeptidases in Streptomyces lividans 66.";
RL J. Ind. Microbiol. 13:24-29(1994).
CC -!- FUNCTION: Hydrolyzes preferentially the N-terminal glycine and can also
CC hydrolyze other amino acids which are used by PepN but is unable to
CC hydrolyze basic amino acids.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; L23173; AAA26695.1; -; Genomic_DNA.
DR AlphaFoldDB; Q54340; -.
DR MEROPS; M01.012; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Aminopeptidase; Cytoplasm; Hydrolase; Metalloprotease; Protease; Zinc.
FT CHAIN <1..>73
FT /note="Aminopeptidase G"
FT /id="PRO_0000095077"
FT REGION 39..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT NON_TER 73
SQ SEQUENCE 73 AA; 8125 MW; A361F9A00D3C9C95 CRC64;
LQMLHAWTNS ALVHYAAPDW RETGGRLLGE GALRELRDGR RAASSSWPGR GSSRRWRPGR
RTGAAARGCW RAP