(data stored in SCRATCH zone)

SWISSPROT: Q47SM6_THEFY

ID   Q47SM6_THEFY            Unreviewed;       501 AA.
AC   Q47SM6;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 104.
DE   RecName: Full=Probable cytosol aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181};
DE            EC=3.4.11.1 {ECO:0000256|HAMAP-Rule:MF_00181};
DE   AltName: Full=Leucine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181};
DE            Short=LAP {ECO:0000256|HAMAP-Rule:MF_00181};
DE            EC=3.4.11.10 {ECO:0000256|HAMAP-Rule:MF_00181};
DE   AltName: Full=Leucyl aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181};
GN   Name=pepA {ECO:0000256|HAMAP-Rule:MF_00181};
GN   OrderedLocusNames=Tfu_0503 {ECO:0000313|EMBL:AAZ54541.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54541.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Presumably involved in the processing and regular
CC       turnover of intracellular proteins. Catalyzes the removal of
CC       unsubstituted N-terminal amino acids from various peptides.
CC       {ECO:0000256|HAMAP-Rule:MF_00181, ECO:0000256|SAAS:SAAS00727879}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which
CC         Xaa is preferably Leu, but may be other amino acids including
CC         Pro although not Arg or Lys, and Yaa may be Pro. Amino acid
CC         amides and methyl esters are also readily hydrolyzed, but rates
CC         on arylamides are exceedingly low.; EC=3.4.11.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00181,
CC         ECO:0000256|SAAS:SAAS01118307};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, preferentially
CC         leucine, but not glutamic or aspartic acids.; EC=3.4.11.10;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00181};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00181};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00181};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00181,
CC       ECO:0000256|SAAS:SAAS00759153}.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00181, ECO:0000256|SAAS:SAAS00754360}.
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DR   EMBL; CP000088; AAZ54541.1; -; Genomic_DNA.
DR   STRING; 269800.Tfu_0503; -.
DR   EnsemblBacteria; AAZ54541; AAZ54541; Tfu_0503.
DR   KEGG; tfu:Tfu_0503; -.
DR   eggNOG; ENOG4105BZ6; Bacteria.
DR   eggNOG; COG0260; LUCA.
DR   HOGENOM; HOG000243129; -.
DR   KO; K01255; -.
DR   OMA; DSPANQM; -.
DR   Proteomes; UP000000434; Chromosome.
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; Q47SM6.
DR   SWISS-2DPAGE; Q47SM6.
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181,
KW   ECO:0000256|SAAS:SAAS00754331, ECO:0000313|EMBL:AAZ54541.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00181,
KW   ECO:0000256|SAAS:SAAS00759165};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00181,
KW   ECO:0000256|SAAS:SAAS00754382, ECO:0000313|EMBL:AAZ54541.1};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00181,
KW   ECO:0000256|SAAS:SAAS00727876};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00181,
KW   ECO:0000256|SAAS:SAAS00754372};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00181,
KW   ECO:0000256|SAAS:SAAS00754389};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434}.
FT   DOMAIN      346    353       CYTOSOL_AP. {ECO:0000259|PROSITE:
FT                                PS00631}.
FT   ACT_SITE    278    278       {ECO:0000256|HAMAP-Rule:MF_00181}.
FT   ACT_SITE    352    352       {ECO:0000256|HAMAP-Rule:MF_00181}.
FT   METAL       266    266       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00181}.
FT   METAL       271    271       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00181}.
FT   METAL       271    271       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00181}.
FT   METAL       289    289       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00181}.
FT   METAL       348    348       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00181}.
FT   METAL       350    350       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00181}.
FT   METAL       350    350       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00181}.
SQ   SEQUENCE   501 AA;  51905 MW;  7AF3C09C10E63F81 CRC64;
     MPVPLATEIH PTDGVLAEST ADRLAIIVRA GTDGPQPVAD GVGLSLTNLD ARLPASVAQL
     FDTYEFRGKA GQIVEFPVDL GRGLIRLSFL GVGDATPEEM RKAGAAFARS VRGSSRAAVN
     AAVSGHDPEA LTAFVEGALL ASYTFTLTET AEGTAPAAAI DLVGSAASEA AEPTRRGTVL
     ARATAMARDL INTPAAEKSP AWLASRAEAI GAEAGLSVRV WDEEALYHDG FGAILTVGQG
     SPRPPRLVEL SYRPAGATEH IVLVGKGITF DTGGLSLKPN DNMKLMKTDM SGAGIILAVL
     SAVQELGVRV SVTGLLAIAE NAFSGSAMRL GDVLTTYSGR TVEVLNSDAE GRLVLADAIG
     YAVTKLAPDT LVDVATLTGA ARVALGSGIG ALFATDDTLA AALVDAGKRS GETLWRMPLH
     EEYRDALDSP VADLANTSVK DDYGHPGAIE AALFLREFVG SVPWAHLDIA GPGRSMSDEG
     ILSKGGTAFG TRLLLRWLAE R
//

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