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METN_VIBCH
ID   METN_VIBCH              Reviewed;         344 AA.
AC   Q9KTJ5;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=VC_0907;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003852; AAF94069.1; -; Genomic_DNA.
DR   PIR; C82266; C82266.
DR   RefSeq; NP_230554.1; NC_002505.1.
DR   RefSeq; WP_000569878.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KTJ5; -.
DR   SMR; Q9KTJ5; -.
DR   STRING; 243277.VC_0907; -.
DR   DNASU; 2614198; -.
DR   EnsemblBacteria; AAF94069; AAF94069; VC_0907.
DR   GeneID; 57739599; -.
DR   KEGG; vch:VC_0907; -.
DR   PATRIC; fig|243277.26.peg.864; -.
DR   eggNOG; COG1135; Bacteria.
DR   HOGENOM; CLU_000604_1_3_6; -.
DR   OMA; VFITHEI; -.
DR   BioCyc; VCHO:VC0907-MON; -.
DR   Proteomes; UP000000584; 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   3: Inferred from homology;
KW   Amino-acid transport; ATP-binding; Cell inner membrane; Cell membrane;
KW   Membrane; Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..344
FT                   /note="Methionine import ATP-binding protein MetN"
FT                   /id="PRO_0000092511"
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   344 AA;  37574 MW;  40D60D2C0CF52913 CRC64;
     MIEIKSVNKV FYQGDKQIHA LKDINLFIPQ GTIFGVIGSS GAGKSTLIRC VNMLEKPTSG
     QVIVDGVDLT TLSNPQLCAA RRNIGMIFQH FNLLSSRTVF ENVALPLELA GQSQQHIETK
     VTELLALVGL SEKRESYPAN LSGGQKQRVA IARALASDPK VLLCDEATSA LDPATTQSIL
     ELLKEINRQL NLTILLITHE MDVVKSICHE VAIIGGGELV EKGTVGDIFA HPKTELAHQF
     IRSTLDLSIP EDYQVRLQPT RVAGSYPLVR LEFTGATVDA PLMTQIARKY NIDVSILSSD
     LDYAGGVKFG MMVAEIFGNA DDDEAAIRYL RENNVKVEVL GYVL
 
 
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