METN1_RHOJR
ID METN1_RHOJR Reviewed; 338 AA.
AC Q0SFY5;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Methionine import ATP-binding protein MetN 1 {ECO:0000255|HAMAP-Rule:MF_01719};
DE EC=7.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01719};
GN Name=metN1 {ECO:0000255|HAMAP-Rule:MF_01719};
GN OrderedLocusNames=RHA1_ro01738;
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1;
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG93551.1; -; Genomic_DNA.
DR RefSeq; WP_011594672.1; NC_008268.1.
DR AlphaFoldDB; Q0SFY5; -.
DR SMR; Q0SFY5; -.
DR STRING; 101510.RHA1_ro01738; -.
DR EnsemblBacteria; ABG93551; ABG93551; RHA1_ro01738.
DR KEGG; rha:RHA1_ro01738; -.
DR PATRIC; fig|101510.16.peg.1758; -.
DR eggNOG; COG1135; Bacteria.
DR HOGENOM; CLU_000604_1_3_11; -.
DR OMA; VIRKICH; -.
DR Proteomes; UP000008710; 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 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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43166:SF5; PTHR43166:SF5; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 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 membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..338
FT /note="Methionine import ATP-binding protein MetN 1"
FT /id="PRO_0000270368"
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"
SQ SEQUENCE 338 AA; 36030 MW; F6A7EC8483FA65F9 CRC64;
MIEVRSVTKR FGKGSRSVEV LHDIDFSVGT GQIAAVIGQS GAGKTTLSRI ISLLERPSEG
RILLDGTDVS GLSERRLRDQ RRAIGTIFQA SSLLARRTAA ENVALPLEFA GVGRSERRAR
VAELLGRVGL SDKADLYPRQ LSGGQRQRVG IARSLALAPK VLVSDEATSG LDPNTTRSIL
ALLRELRDDL GLTIVLITHE MDVVRQVADV VTVLDAGRVV ESGPVIELLR DPHSELGVGL
LPDRSHITAE DRDVLWHVTY GSDTVPTNWI ELLGKATGRS IGVLSGTVES VGGRPAGRVT
ISVAGEHPSV GDLLSSWGLH GTRVDDDASA RTTEEAAA