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 13-NOV-2019, entry version 87. 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 CC transport system. {ECO:0000255|HAMAP-Rule:MF_01719}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + L-methionine(out) = ADP + H(+) + L- CC methionine(in) + phosphate; Xref=Rhea:RHEA:29779, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:456216; CC EC=7.4.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_01719}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + D-methionine(out) + H2O = ADP + D-methionine(in) + CC H(+) + 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 CC (MetN), two transmembrane proteins (MetI) and a solute-binding CC protein (MetQ). {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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF102556; AAD51880.1; -; Genomic_DNA. DR SMR; Q9S4Z0; -. 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 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; 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; KW Amino-acid transport; ATP-binding; Cell inner membrane; Cell membrane; KW Membrane; Nucleotide-binding; Translocase; Transport. FT CHAIN 1 315 Methionine import ATP-binding protein FT MetN. FT /FTId=PRO_0000270377. FT DOMAIN 2 219 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01719}. FT NP_BIND 16 23 ATP. {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 //