METN2_STAAM
ID METN2_STAAM Reviewed; 341 AA.
AC Q99VG8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
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=SAV0837;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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}.
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DR EMBL; BA000017; BAB56999.1; -; Genomic_DNA.
DR RefSeq; WP_000571207.1; NC_002758.2.
DR PDB; 3CED; X-ray; 2.15 A; A/B/C=247-341.
DR PDBsum; 3CED; -.
DR AlphaFoldDB; Q99VG8; -.
DR SMR; Q99VG8; -.
DR World-2DPAGE; 0002:Q99VG8; -.
DR PaxDb; Q99VG8; -.
DR EnsemblBacteria; BAB56999; BAB56999; SAV0837.
DR KEGG; sav:SAV0837; -.
DR HOGENOM; CLU_000604_1_3_9; -.
DR OMA; VIRKICH; -.
DR PhylomeDB; Q99VG8; -.
DR BioCyc; SAUR158878:SAV_RS04575-MON; -.
DR EvolutionaryTrace; Q99VG8; -.
DR Proteomes; UP000002481; 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; Translocase; Transport.
FT CHAIN 1..341
FT /note="Methionine import ATP-binding protein MetN 2"
FT /id="PRO_0000270396"
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 247..255
FT /evidence="ECO:0007829|PDB:3CED"
FT STRAND 264..274
FT /evidence="ECO:0007829|PDB:3CED"
FT HELIX 276..287
FT /evidence="ECO:0007829|PDB:3CED"
FT STRAND 292..301
FT /evidence="ECO:0007829|PDB:3CED"
FT STRAND 304..314
FT /evidence="ECO:0007829|PDB:3CED"
FT HELIX 318..330
FT /evidence="ECO:0007829|PDB:3CED"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:3CED"
SQ SEQUENCE 341 AA; 38259 MW; 9E14C5F116943E48 CRC64;
MIELKEVVKE YRTKNKEVLA VDHVNLSIRA GSIYGVIGFS GAGKSTLIRM FNHLEAPTSG
EVIIDGDHIG QLSKNGLRAK RQKVNMIFQH FNLLWSRTVL KNIMFPLEIA GVPRRRAKQK
ALELVELVGL KGREKAYPSE LSGGQKQRVG IARALANDPT VLLCDEATSA LDPQTTDEIL
DLLLKIREQQ NLTIVLITHE MHVIRRICDE VAVMESGKVI EHGPVTQVFE NPQHTVTKRF
VKEDLNDDFE TSLTELEPLE KDAYIVRLVF AGSTTTEPIV SSLSTAYDIK INILEANIKN
TKNGTVGFLV LHIPYISSVD FGKFEKELIE RQVKMEVLRH G
