MDTH_SALPA
ID MDTH_SALPA Reviewed; 402 AA.
AC Q5PGW7;
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 MdtH {ECO:0000255|HAMAP-Rule:MF_01529};
GN Name=mdtH {ECO:0000255|HAMAP-Rule:MF_01529}; OrderedLocusNames=SPA1685;
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_01529}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01529}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family.
CC MdtH (TC 2.A.1.2.21) subfamily. {ECO:0000255|HAMAP-Rule:MF_01529}.
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; AAV77610.1; -; Genomic_DNA.
DR RefSeq; WP_000092178.1; NC_006511.1.
DR AlphaFoldDB; Q5PGW7; -.
DR SMR; Q5PGW7; -.
DR EnsemblBacteria; AAV77610; AAV77610; SPA1685.
DR KEGG; spt:SPA1685; -.
DR HOGENOM; CLU_001265_60_2_6; -.
DR OMA; TVCVWTL; -.
DR Proteomes; UP000008185; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.1250.20; -; 1.
DR HAMAP; MF_01529; MFS_MdtH; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR022855; Multidrug-R_MdtH.
DR Pfam; PF07690; MFS_1; 2.
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..402
FT /note="Multidrug resistance protein MdtH"
FT /id="PRO_0000173348"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TOPO_DOM 34..98
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 99..116
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TOPO_DOM 117..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TOPO_DOM 160..164
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TOPO_DOM 186..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TOPO_DOM 235..243
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TOPO_DOM 265..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TOPO_DOM 298..299
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TOPO_DOM 321..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TOPO_DOM 361..367
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TOPO_DOM 389..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
SQ SEQUENCE 402 AA; 44384 MW; E50CEA555A6451CD CRC64;
MSRVSQARNL GKYFLLIDNM LVVLGFFVVF PLISIRFVDQ MGWAAVMVGI ALGLRQFIQQ
GLGIFGGAIA DRFGAKPMIV TGMLMRAAGF ATMGIAHEPW LLWFSCFLSG LGGTLFDPPR
SALVVKLIRP EQRGRFFSLL MMQDSAGAVI GALLGSWLLQ YDFRLVCATG AILFILCALF
NAWLLPAWKL STVRTPVREG MRRVMSDKRF VTYVLTLAGY YMLAVQVMLM LPIMVNDIAG
SPAAVKWMYA IEACLSLTLL YPIARWSEKR FRLEHRLMAG LLVMSLSMLP IGMVGNLQQL
FTLICAFYIG SVIAEPARET LSASLADARA RGSYMGFSRL GLAIGGAIGY IGGGWLFDMG
KALAQPELPW MMLGIIGFIT FLALGWQFSH KRTPRRMLEP GA
