METN1_SALPA
ID METN1_SALPA Reviewed; 343 AA.
AC Q5PID0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
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}; OrderedLocusNames=SPA0254;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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}.
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; CP000026; AAV76283.1; -; Genomic_DNA.
DR RefSeq; WP_000594015.1; NC_006511.1.
DR AlphaFoldDB; Q5PID0; -.
DR SMR; Q5PID0; -.
DR EnsemblBacteria; AAV76283; AAV76283; SPA0254.
DR KEGG; spt:SPA0254; -.
DR HOGENOM; CLU_000604_1_3_6; -.
DR OMA; VFITHEI; -.
DR Proteomes; UP000008185; Chromosome.
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; Translocase; Transport.
FT CHAIN 1..343
FT /note="Methionine import ATP-binding protein MetN 1"
FT /id="PRO_0000270378"
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 343 AA; 37634 MW; 0BF9F7AF6D380174 CRC64;
MIKLSNITKV FQQGARTIQA LNNVSLHVPA GQIYGVIGAS GAGKSTLIRC VNLLERPTEG
SVMVGGQELT TLSESELTKA RRQIGMIFQH FNLLSSRTVF GNVALPLELD NTPKEEIKRR
VTELLDLVGL GDKHDSYPAN LSGGQKQRVA IARALASNPK VLLCDEATSA LDPATTRSIL
ELLKDINRRL GLTILLITHE MDVVKRICDC VAVISNGELI EQDTVSEVFS HPKTPLAQKF
IQSTLHLDIP EDYQARLKAS PETDSVPMLR MEFTGQSVDA PLLSETARRF NVNNNIISAQ
MDYAGGVKFG IMLTEMHGTQ EETQAAIAWL QDHHVKVEVL GYV
