METN_VIBPA
ID METN_VIBPA Reviewed; 344 AA.
AC Q87RS1;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=VP0706;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; BA000031; BAC58969.1; -; Genomic_DNA.
DR RefSeq; NP_797085.1; NC_004603.1.
DR RefSeq; WP_005459161.1; NC_004603.1.
DR PDB; 2QRR; X-ray; 1.71 A; A/B=247-344.
DR PDBsum; 2QRR; -.
DR AlphaFoldDB; Q87RS1; -.
DR SMR; Q87RS1; -.
DR STRING; 223926.28805692; -.
DR EnsemblBacteria; BAC58969; BAC58969; BAC58969.
DR GeneID; 1188181; -.
DR KEGG; vpa:VP0706; -.
DR PATRIC; fig|223926.6.peg.675; -.
DR eggNOG; COG1135; Bacteria.
DR HOGENOM; CLU_000604_1_3_6; -.
DR OMA; VFITHEI; -.
DR EvolutionaryTrace; Q87RS1; -.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro.
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 CDD; cd03258; ABC_MetN_methionine_transporter; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR026253; ABC_MetN.
DR InterPro; IPR012692; ABC_MetN_proteobac.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR045865; ACT-like_dom_sf.
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 SUPFAM; SSF55021; SSF55021; 1.
DR TIGRFAMs; TIGR02314; ABC_MetN; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51264; METN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; ATP-binding; Cell inner membrane;
KW Cell membrane; Membrane; Nucleotide-binding; Reference proteome;
KW Translocase; Transport.
FT CHAIN 1..344
FT /note="Methionine import ATP-binding protein MetN"
FT /id="PRO_0000270435"
FT DOMAIN 2..241
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01719"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01719"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:2QRR"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:2QRR"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:2QRR"
FT HELIX 282..289
FT /evidence="ECO:0007829|PDB:2QRR"
FT STRAND 293..304
FT /evidence="ECO:0007829|PDB:2QRR"
FT STRAND 307..318
FT /evidence="ECO:0007829|PDB:2QRR"
FT HELIX 320..332
FT /evidence="ECO:0007829|PDB:2QRR"
FT STRAND 336..343
FT /evidence="ECO:0007829|PDB:2QRR"
SQ SEQUENCE 344 AA; 37567 MW; 315DB9DF298B40D7 CRC64;
MIEIKNVNKV FYQGSKEILA LKDINLHIAK GTIFGVIGSS GAGKSTLIRC VNMLEAPSSG
SIIVDGVDLT TLSKKQLVET RRNIGMIFQH FNLLSSRTVF DNVALPLELA GKDKSQITTK
VTELLKLVGL ADKHESYPSN LSGGQKQRVA IARALASDPS VLLCDEATSA LDPATTQSIL
ELLKEINRKL NITILLITHE MEVVKSICHE VAIIGGGELV EKGTVGDIFA HPKTELAHEF
IRSTLDLSIP EDYQARLQPN RVEGSYPLVR MEFTGATVDA PLMSQISRKY NIDVSILSSD
LDYAGGVKFG MMVAELFGNE QDDSAAIEYL REHNVKVEVL GYVL
