MDTG_SALPA
ID MDTG_SALPA Reviewed; 404 AA.
AC Q5PGY0;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Multidrug resistance protein MdtG {ECO:0000255|HAMAP-Rule:MF_01528};
GN Name=mdtG {ECO:0000255|HAMAP-Rule:MF_01528}; OrderedLocusNames=SPA1697;
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 -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01528}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01528}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family.
CC MdtG (TC 2.A.1.2.20) subfamily. {ECO:0000255|HAMAP-Rule:MF_01528}.
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DR EMBL; CP000026; AAV77621.1; -; Genomic_DNA.
DR RefSeq; WP_000075043.1; NC_006511.1.
DR AlphaFoldDB; Q5PGY0; -.
DR SMR; Q5PGY0; -.
DR EnsemblBacteria; AAV77621; AAV77621; SPA1697.
DR KEGG; spt:SPA1697; -.
DR HOGENOM; CLU_001265_57_3_6; -.
DR OMA; VIRHNVP; -.
DR Proteomes; UP000008185; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.1250.20; -; 2.
DR HAMAP; MF_01528; MFS_MdtG; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR023692; Mutidrug-R_MdtG.
DR InterPro; IPR001958; Tet-R_TetA/multi-R_MdtG.
DR Pfam; PF07690; MFS_1; 1.
DR PRINTS; PR01035; TCRTETA.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..404
FT /note="Multidrug resistance protein MdtG"
FT /id="PRO_0000173338"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
SQ SEQUENCE 404 AA; 43568 MW; C9BA73F90C0439AD CRC64;
MSPSDVPINW KRNLTVTWLG CFLTGAAFSL VMPFLPLYVE QLGVTGHSAL NMWSGLVFSI
TFLFSAIASP FWGGLADRKG RKIMLLRSAL GMAIVMLLMG MAQNIWQFLI LRALLGLLGG
FIPNANALIA TQAPRHKSGW ALGTLSTGGV SGALLGPLAG GLLADHYGLR PVFFITASVL
FICFLLTFFF IRENFLPVSK KEMLHVREVV ASLKNPRLVL SLFVTTLIIQ VATGSIAPIL
TLYVRELAGN VSNIAFISGM IASVPGVAAL LSAPRLGKLG DRIGPEKILI VALIISVLLL
IPMSFVQTPW QLALLRFLLG AADGALLPAV QTLLVYNSTN QIAGRIFSYN QSFRDIGNVT
GPLMGAAISA SYGFRAVFCV TAGVVLFNAI YSWNSLRRRR LAIE