(data stored in SCRATCH zone)

SWISSPROT: METN_FRAT1

ID   METN_FRAT1              Reviewed;         350 AA.
AC   Q14H97;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   11-DEC-2019, entry version 86.
DE   RecName: Full=Methionine import ATP-binding protein MetN {ECO:0000255|HAMAP-Rule:MF_01719};
DE            EC=7.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01719};
GN   Name=metN {ECO:0000255|HAMAP-Rule:MF_01719}; OrderedLocusNames=FTF1124;
OS   Francisella tularensis subsp. tularensis (strain FSC 198).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=393115;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSC 198;
RX   PubMed=17406676; DOI=10.1371/journal.pone.0000352;
RA   Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J.,
RA   Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E.,
RA   Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.;
RT   "Genome sequencing shows that European isolates of Francisella tularensis
RT   subspecies tularensis are almost identical to US laboratory strain Schu
RT   S4.";
RL   PLoS ONE 2:E352-E352(2007).
CC   -!- FUNCTION: Part of the ABC transporter complex MetNIQ involved in
CC       methionine import. Responsible for energy coupling to the transport
CC       system. {ECO:0000255|HAMAP-Rule:MF_01719}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in)
CC         + phosphate; Xref=Rhea:RHEA:29779, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:456216; EC=7.4.2.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01719};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-methionine(out) + H2O = ADP + D-methionine(in) + H(+)
CC         + phosphate; Xref=Rhea:RHEA:29767, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57932, ChEBI:CHEBI:456216; EC=7.4.2.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01719};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MetN),
CC       two transmembrane proteins (MetI) and a solute-binding protein (MetQ).
CC       {ECO:0000255|HAMAP-Rule:MF_01719}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01719}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01719}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Methionine
CC       importer (TC 3.A.1.24) family. {ECO:0000255|HAMAP-Rule:MF_01719}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAL09140.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AM286280; CAL09140.1; ALT_INIT; Genomic_DNA.
DR   SMR; Q14H97; -.
DR   EnsemblBacteria; CAL09140; CAL09140; FTF1124.
DR   KEGG; ftf:FTF1124; -.
DR   KO; K02071; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0015424; F:ATPase-coupled amino acid transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015821; P:methionine transport; IEA:InterPro.
DR   CDD; cd03258; ABC_MetN_methionine_transporter; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR026253; ABC_MetN.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR017908; ABC_transprt_methionine_MetN_C.
DR   InterPro; IPR041701; MetN_ABC.
DR   InterPro; IPR018449; NIL_domain.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43166:SF5; PTHR43166:SF5; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF09383; NIL; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00930; NIL; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51264; METN; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q14H97.
DR   SWISS-2DPAGE; Q14H97.
KW   Amino-acid transport; ATP-binding; Cell inner membrane; Cell membrane;
KW   Membrane; Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..350
FT                   /note="Methionine import ATP-binding protein MetN"
FT                   /id="PRO_0000270303"
FT   DOMAIN          2..241
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01719"
FT   NP_BIND         38..45
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01719"
SQ   SEQUENCE   350 AA;  39074 MW;  935E57F2070C8F47 CRC64;
     MIQIKNLKKE YRTNNTSNLV LDNINLEIKQ GEIFGIIGHS GAGKSSLLRC LNLLEQPTDG
     SIFIADENIT KKNSKQLREF RKKVAMIFQH FNLLSSRNVF ENIALPLEIQ GIPKSEIKKR
     VFELLDLVEL PNKANAYPQE LSGGQKQKVA IARALALNPL VLLSDEATSA LDPTSTKQIL
     ALLKILNKEL GLTIVLITHE IDVVRKICDR VAIIDKGRIA EMGKTLDVFL NPQAPVTRSF
     VETSIHTKVP DFIAKKLQDN PYSYDNTYPV VQLTFYGDKG KMPIIAEISR QFNATASIIQ
     ANIETIQDQI VGIAICHITG ERQGWENALR FLSNQDVNLK VLGYATADNI
//

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