AMPA_MYCGE
ID AMPA_MYCGE Reviewed; 447 AA.
AC P47631; Q49371;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable cytosol aminopeptidase;
DE EC=3.4.11.1;
DE AltName: Full=Leucine aminopeptidase;
DE Short=LAP;
DE EC=3.4.11.10;
DE AltName: Full=Leucyl aminopeptidase;
GN Name=pepA; OrderedLocusNames=MG391;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72 AND 138-245.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
CC -!- FUNCTION: Presumably involved in the processing and regular turnover of
CC intracellular proteins. Catalyzes the removal of unsubstituted N-
CC terminal amino acids from various peptides (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC is preferably Leu, but may be other amino acids including Pro
CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC methyl esters are also readily hydrolyzed, but rates on arylamides
CC are exceedingly low.; EC=3.4.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, preferentially leucine,
CC but not glutamic or aspartic acids.; EC=3.4.11.10;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD12535.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L43967; AAC71619.1; -; Genomic_DNA.
DR EMBL; U02268; AAD12535.1; ALT_INIT; Genomic_DNA.
DR EMBL; U01801; AAD12327.1; -; Genomic_DNA.
DR EMBL; U01802; AAD12328.1; -; Genomic_DNA.
DR PIR; C64243; C64243.
DR RefSeq; WP_009885632.1; NZ_AAGX01000001.1.
DR AlphaFoldDB; P47631; -.
DR SMR; P47631; -.
DR STRING; 243273.MG_391; -.
DR EnsemblBacteria; AAC71619; AAC71619; MG_391.
DR KEGG; mge:MG_391; -.
DR eggNOG; COG0260; Bacteria.
DR HOGENOM; CLU_013734_6_3_14; -.
DR OMA; QWAFAQG; -.
DR OrthoDB; 356206at2; -.
DR BioCyc; MGEN243273:G1GJ2-487-MON; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00433; Peptidase_M17; 1.
DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR PANTHER; PTHR11963; PTHR11963; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Cytoplasm; Hydrolase; Manganese; Metal-binding; Protease;
KW Reference proteome.
FT CHAIN 1..447
FT /note="Probable cytosol aminopeptidase"
FT /id="PRO_0000165766"
FT ACT_SITE 230
FT /evidence="ECO:0000255"
FT ACT_SITE 304
FT /evidence="ECO:0000255"
FT BINDING 218
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 447 AA; 49107 MW; 2AFCABC9C10477E3 CRC64;
MRINKPFSDD SNTVVFVSSK TYGVKEEAAH NPNVEFGVVL PTDFPAFNRA LVQFLKRKKT
KLNINLDSLI ELYKKNENSG CFHTAIKTVI TSVTFCETTP FTMKTKPEKN VEVAVQCAVE
YHNLVKEYET VGEYVNLARE LQDTPSDLLY SEVFVKHFEK AASKLPVKIK VLKQSDLIKK
KMGLLLGVNQ GSEREARLLV ISYQANKNSK EKLAFVGKGI TYDSGGMNIK TGDYMRGMKY
DMSGAAIVCS TVLALAKNKV KTNVVAVAAL TENLPGAKAQ RPDDIKIAYN GKSVEIDNTD
AEGRLVLADA ITYAAKDLAA THIIDVATLT GLMSYILSTT YTGIFSTCDH QWESFKKAAC
SAGEPVWRLP MHPDYLKPLQ LTKLADLQNS TSARGAGSSR AACFLAEFRE GVSLIHCDIA
STASIENLGQ GVLVRTLYER ASQLANK
