AMPA_AERPE
ID AMPA_AERPE Reviewed; 492 AA.
AC Q9Y935;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 104.
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=APE_2450.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
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}.
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DR EMBL; BA000002; BAA81465.2; -; Genomic_DNA.
DR PIR; A72476; A72476.
DR AlphaFoldDB; Q9Y935; -.
DR SMR; Q9Y935; -.
DR STRING; 272557.APE_2450.1; -.
DR EnsemblBacteria; BAA81465; BAA81465; APE_2450.1.
DR KEGG; ape:APE_2450.1; -.
DR PATRIC; fig|272557.25.peg.1627; -.
DR eggNOG; arCOG04322; Archaea.
DR Proteomes; UP000002518; 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..492
FT /note="Probable cytosol aminopeptidase"
FT /id="PRO_0000165822"
FT ACT_SITE 260
FT /evidence="ECO:0000255"
FT ACT_SITE 334
FT /evidence="ECO:0000255"
FT BINDING 248
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 492 AA; 52387 MW; BA7A346C04D16260 CRC64;
MVLYTRPPRL SVSRETFFGR QTPVVIPVFK EGDSIKLPEG LPQDLESLLK ESYNSKAVSP
EPGSVAKLPY RGGLVVTAGC GAPGDLEGVR RGFAAASRQV VDSFEEAQLY LVGLDTVSST
EAVIGALLGA YRLEEFKNTR KRKLQQLWVY GGEPRLDYAQ AVAEGVYLAR DIANAPPHRL
PPAKLAAAVE DLFSKFDNVD VEVFSYDRLL EEGFGGIVSV GMGSEEKPRL IIIKYRGGAG
EPIALVGKAV VFDSGGINLK PSQGMTLMRA DKAGGAAVVG AMWTAARLGI KASIIGLIPA
VINVPSGSSY LPSDVIRMWD GTMVEITNTD AEGRLILADA ISYAAKQLGA KTVIDLATLT
GAIVVALGPL IAGLFTRSDG LARAFEEASR TTGEKIWRMP MEDEYAKSLT QPAQAGEIVN
AAQRYGGAIF GALFLERFVH GKEFAHLDIA GPGIAFEAGS LAPPYWPEKG MAPGYGVRLL
IEVLSRMARG GG
