METN_SALEN
ID METN_SALEN Reviewed; 315 AA.
AC Q9S4Z0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 94.
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}; Synonyms=sfbB;
OS Salmonella enteritidis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=149539;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S1400;
RX PubMed=10447888; DOI=10.1046/j.1365-2958.1999.01526.x;
RA Pattery T., Hernalsteens J.-P., De Greve H.;
RT "Identification and molecular characterization of a novel Salmonella
RT enteritidis pathogenicity islet encoding an ABC transporter.";
RL Mol. Microbiol. 33:791-805(1999).
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}.
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DR EMBL; AF102556; AAD51880.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9S4Z0; -.
DR SMR; Q9S4Z0; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033232; F:ABC-type D-methionine transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR026253; ABC_MetN.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR045865; ACT-like_dom_sf.
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 SUPFAM; SSF55021; SSF55021; 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;
KW Amino-acid transport; ATP-binding; Cell inner membrane; Cell membrane;
KW Membrane; Nucleotide-binding; Translocase; Transport.
FT CHAIN 1..315
FT /note="Methionine import ATP-binding protein MetN"
FT /id="PRO_0000270377"
FT DOMAIN 2..219
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01719"
FT BINDING 16..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01719"
SQ SEQUENCE 315 AA; 34141 MW; 89D8C257EE5757BF CRC64;
MIEIEKVCVD FTAGRGTSGA GKSTLLRTLN ALTRPSQGRV NVNGVEISAL DGKALRQARQ
RIGMIFQHFN LMHTRTVAQN VAFSLKAAGW ERSKIAPRVA EILTLVGLAD KANRFPVQLS
GGQKQRVGIA RAIANHPDVL LCDEPTSALD LETSATILAL LRQINAQLGI TIVLITHEMN
VIKSICDRVA VMSGGKVVES GEVFDEFAHP QHAFTQQLVS HTLNLTLPER LREHLPGQLL
KILFIGDSAE QPVLSEVAIK FGVAVNILHG KIEYIGERAL GILVVQLTAP HNPTAVAAAV
EHIRQRTAQV EVIRG