AMPA_ACIF2
ID AMPA_ACIF2 Reviewed; 500 AA.
AC B7J5I9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Probable cytosol aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181};
DE EC=3.4.11.1 {ECO:0000255|HAMAP-Rule:MF_00181};
DE AltName: Full=Leucine aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181};
DE Short=LAP {ECO:0000255|HAMAP-Rule:MF_00181};
DE EC=3.4.11.10 {ECO:0000255|HAMAP-Rule:MF_00181};
DE AltName: Full=Leucyl aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181};
GN Name=pepA {ECO:0000255|HAMAP-Rule:MF_00181}; OrderedLocusNames=AFE_2201;
OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=243159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455;
RX PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II,
RA Eisen J.A., Holmes D.S.;
RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT industrial applications.";
RL BMC Genomics 9:597-597(2008).
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. {ECO:0000255|HAMAP-
CC Rule:MF_00181}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00181};
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00181};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00181};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00181};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00181}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000255|HAMAP-
CC Rule:MF_00181}.
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DR EMBL; CP001219; ACK79866.1; -; Genomic_DNA.
DR RefSeq; WP_009567190.1; NC_011761.1.
DR AlphaFoldDB; B7J5I9; -.
DR SMR; B7J5I9; -.
DR STRING; 243159.AFE_2201; -.
DR MEROPS; M17.003; -.
DR PaxDb; B7J5I9; -.
DR EnsemblBacteria; ACK79866; ACK79866; AFE_2201.
DR GeneID; 66432961; -.
DR KEGG; afr:AFE_2201; -.
DR eggNOG; COG0260; Bacteria.
DR HOGENOM; CLU_013734_2_2_6; -.
DR OMA; MKNTGPR; -.
DR OrthoDB; 356206at2; -.
DR Proteomes; UP000001362; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963; PTHR11963; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; SSF52949; 1.
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..500
FT /note="Probable cytosol aminopeptidase"
FT /id="PRO_1000118444"
FT ACT_SITE 281
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT ACT_SITE 355
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 269
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 274
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 274
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 292
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 351
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 353
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 353
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
SQ SEQUENCE 500 AA; 52844 MW; 7E950A380AC66BF1 CRC64;
MEIAVQCQNP TTDNSDCVVV GIYEGGILSP AATLVDLASG GALRALLDTG DFTGDCGDTQ
LLYQVPGMAA ARVLVLGLGS HGKVKDSQFR KAALAAARAL QGARVGRASL HLLDTPVIRR
SAPACAKILV QAVADAEYHF DRHKKPADAP QRPISELQLS ISENDTAALA ELQGAVAEAQ
ATARAVAWTR DMANEPGNIC TPTWLAEQAE AMAGRLGIKS TILGPDAMEA LGMHLLLGVA
HGSRQPPRLI ILEYRGGAEN QAPIVLVGKG ITFDAGGISL KPADKMDEMK YDMCGGASAL
AAIQAAAELQ LPLNIVTVVP ASENLPDGQA TKPGDIHRSM NGLSVEVVNT DAEGRLILAD
TLTYVERFEP DVVIDMATLT GACIIALGHQ TAAVMGNHEG LVHDLIAAGK ESMDRVWELP
LFEEYQEQLK SPVADLSNVG GRPAGTITAA CFLSRFTENY RWAHLDIAGV AWKSGEHKGA
TGRPVPLLVE YLLRRARQVA
