METN2_ENTFA
ID METN2_ENTFA Reviewed; 345 AA.
AC Q831K6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Methionine import ATP-binding protein MetN 2 {ECO:0000255|HAMAP-Rule:MF_01719};
DE EC=7.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01719};
GN Name=metN2 {ECO:0000255|HAMAP-Rule:MF_01719}; OrderedLocusNames=EF_2498;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(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 membrane {ECO:0000255|HAMAP-Rule:MF_01719};
CC Peripheral membrane protein {ECO:0000255|HAMAP-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; AE016830; AAO82214.1; -; Genomic_DNA.
DR RefSeq; NP_816144.1; NC_004668.1.
DR RefSeq; WP_002356639.1; NZ_KE136528.1.
DR PDB; 2QSW; X-ray; 1.50 A; A=249-345.
DR PDBsum; 2QSW; -.
DR AlphaFoldDB; Q831K6; -.
DR SMR; Q831K6; -.
DR STRING; 226185.EF_2498; -.
DR EnsemblBacteria; AAO82214; AAO82214; EF_2498.
DR GeneID; 60894542; -.
DR KEGG; efa:EF2498; -.
DR PATRIC; fig|226185.45.peg.1050; -.
DR eggNOG; COG1135; Bacteria.
DR HOGENOM; CLU_000604_1_3_9; -.
DR OMA; VIRKICH; -.
DR EvolutionaryTrace; Q831K6; -.
DR Proteomes; UP000001415; Chromosome.
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; 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 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; ATP-binding; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..345
FT /note="Methionine import ATP-binding protein MetN 2"
FT /id="PRO_0000270293"
FT DOMAIN 4..243
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01719"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01719"
FT HELIX 258..264
FT /evidence="ECO:0007829|PDB:2QSW"
FT STRAND 267..277
FT /evidence="ECO:0007829|PDB:2QSW"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:2QSW"
FT STRAND 295..306
FT /evidence="ECO:0007829|PDB:2QSW"
FT STRAND 309..320
FT /evidence="ECO:0007829|PDB:2QSW"
FT HELIX 322..334
FT /evidence="ECO:0007829|PDB:2QSW"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:2QSW"
SQ SEQUENCE 345 AA; 38615 MW; 4194CF9C5DD2C489 CRC64;
MALIELRHVK KEFSGKAGKV TALKDIDLTV ESGDIYGIIG YSGAGKSTLV RLLNGLETPT
EGEVEIQGQD IALLPNKELR NFRKKIGMIF QHFNLLWSRT VLENIMLPLE IAGVPKQNRK
SRAEELIKLV GLEGRETAYP SQLSGGQKQR VGIARALANN PDILLCDEAT SALDPQTTDE
VLELLLKINQ ELNLTVVLIT HEMHVIRKIC NRVAVMEYGE IVEEGKVIDI FKKPQTEIAK
RFIQQEADKN IEETELVVEE MLEQYPNGKI VRLLFHGEQA KLPIISHIVQ EYQVEVSIIQ
GNIQQTKQGA VGSLYIQLLG EEQNILAAIE GLRKLRVETE VIGNE
