METN_STRMU
ID METN_STRMU Reviewed; 354 AA.
AC Q93DA2; Q7CE87;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
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=atmD;
GN OrderedLocusNames=SMU_1939c;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT11;
RX PubMed=12161466; DOI=10.1177/154405910208100715;
RA Tao L., Tanzer J.M.;
RT "Novel sucrose-dependent adhesion co-factors in Streptococcus mutans.";
RL J. Dent. Res. 81:505-510(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AF397166; AAL04079.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN59549.1; -; Genomic_DNA.
DR RefSeq; NP_722243.1; NC_004350.2.
DR RefSeq; WP_002262135.1; NC_004350.2.
DR AlphaFoldDB; Q93DA2; -.
DR SMR; Q93DA2; -.
DR STRING; 210007.SMU_1939c; -.
DR PRIDE; Q93DA2; -.
DR EnsemblBacteria; AAN59549; AAN59549; SMU_1939c.
DR GeneID; 66818725; -.
DR KEGG; smu:SMU_1939c; -.
DR PATRIC; fig|210007.7.peg.1724; -.
DR eggNOG; COG1135; Bacteria.
DR HOGENOM; CLU_000604_1_3_9; -.
DR OMA; VFITHEI; -.
DR PhylomeDB; Q93DA2; -.
DR Proteomes; UP000002512; 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; IPR026253; ABC_MetN.
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 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..354
FT /note="Methionine import ATP-binding protein MetN"
FT /id="PRO_0000270414"
FT DOMAIN 8..250
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01719"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01719"
SQ SEQUENCE 354 AA; 39166 MW; 03408E327A516B9A CRC64;
MSKAIIKLDH IDITFHQKKR TIEAVKGVTV HINQGDIYGI VGYSGAGKST LVRVINLLQT
PTKGKITVDQ DVIFENGEKR LSSQELRKKR HEIGMIFQHF NLMAQKTARQ NVAFALRHSN
LSAAQKESKV TELLELVGLT DRAENYPSQL SGGQKQRVAI ARALANDPKI LISDEATSAL
DPKTTKQILA LLQDLNKKLG LTVVMITHEM QIVKDICNRV AVMQEGSLIE EGSVLDIFSN
PREDLTKDFI KTATGIEEAL IKIKQQEIVK NLPANAALVQ LKYAGKTTDE PILNNLYKKY
QVTANILYGN IEILEKTPVG EMIVILEGAA TNIDQALNDL THSDLTVTVL KRGV
