(data stored in ACNUC30630 zone)

SWISSPROT: AMPA_TROW8

ID   AMPA_TROW8              Reviewed;         502 AA.
AC   Q83I32;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   11-DEC-2019, entry version 89.
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=TW261;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(2003).
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}.
DR   EMBL; BX251410; CAD66937.1; -; Genomic_DNA.
DR   RefSeq; WP_011096218.1; NC_004551.1.
DR   SMR; Q83I32; -.
DR   PRIDE; Q83I32; -.
DR   EnsemblBacteria; CAD66937; CAD66937; TW261.
DR   GeneID; 29578443; -.
DR   KEGG; tws:TW261; -.
DR   HOGENOM; HOG000243129; -.
DR   KO; K01255; -.
DR   OMA; MKNTGPR; -.
DR   BioCyc; GCF_000196075:G1EE9-283-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProtKB-UniRule.
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   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   PROSITE; PS00631; CYTOSOL_AP; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q83I32.
DR   SWISS-2DPAGE; Q83I32.
KW   Aminopeptidase; Cytoplasm; Hydrolase; Manganese; Metal-binding; Protease.
FT   CHAIN           1..502
FT                   /note="Probable cytosol aminopeptidase"
FT                   /id="PRO_0000165807"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   ACT_SITE        340
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   METAL           254
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   METAL           259
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   METAL           259
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   METAL           277
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   METAL           336
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   METAL           338
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT   METAL           338
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
SQ   SEQUENCE   502 AA;  53336 MW;  5249BECC6BD06C73 CRC64;
     MSDYTNTVTV EITSDDSLVA DVIVVPVASG AVPRLPEDSK FRAYEDILQK LGVTGSKDEL
     TRIPLDGSKH VVLAFIGVGK AFSATELMFA AGSAVRQIGA RCIQIDFSVT QKDKLSAIVE
     GAFLGAYRFD KYRSKKSECP EVIRVSHNIN GITDSECRQI IARAKVIAGS VGLAKDLVNT
     TGDDLYPAQF ASFVAKDLEG IDHISVESWD EKRLQEKSCG GILGVGRGSN FPPRLVKISY
     TPGQYKKHLS LVGKGITFDT GGLSLKPASA MLGMKYDMTG AANVFAVLRI VALLRLSVRV
     TGWLCLAENM LSGSAIRPGD ILRTYSGKTV EVTNTDAEGR LVLADGLALA GDERPDVIID
     IATLTGAAKV ALGESCSGLM GNNPDLLCSL EVAAKSVGEK FLAVPIDDDA LQKALKSDIA
     DIVNVPTSNK VPGMQFGAVF LKEFETTNDS GEAIPWAHLD VAGPANASYD TGFNSCGPTG
     VAVRSLVEFC RCLSSAPERK LF
//

If you have problems or comments...

PBIL Back to PBIL home page