ID   GSID_SALPA              Reviewed;         303 AA.
AC   Q5PGP6;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Glutathione transport system permease protein GsiD {ECO:0000250|UniProtKB:P75799};
GN   Name=gsiD {ECO:0000250|UniProtKB:P75799}; OrderedLocusNames=SPA1904;
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 GsiABCD involved in
CC       glutathione import. Probably responsible for the translocation of the
CC       substrate across the membrane. {ECO:0000250|UniProtKB:P75799}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (GsiA),
CC       two transmembrane proteins (GsiC and GsiD) and a solute-binding protein
CC       (GsiB). {ECO:0000250|UniProtKB:P75799}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P75799}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. {ECO:0000305}.
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DR   EMBL; CP000026; AAV77815.1; -; Genomic_DNA.
DR   RefSeq; WP_001236024.1; NC_006511.1.
DR   AlphaFoldDB; Q5PGP6; -.
DR   EnsemblBacteria; AAV77815; AAV77815; SPA1904.
DR   KEGG; spt:SPA1904; -.
DR   HOGENOM; CLU_028518_5_3_6; -.
DR   OMA; RAWWVVS; -.
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:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   InterPro; IPR025966; OppC_N.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   Pfam; PF12911; OppC_N; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..303
FT                   /note="Glutathione transport system permease protein GsiD"
FT                   /id="PRO_0000280009"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          101..290
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   303 AA;  33144 MW;  C13BEF6887E6E4BF CRC64;
     MRLFNWRRQA ILHAMPVVKP DQIRTPWREF WRRFRRQHVA LVAGGFVLAL ILVAIFARWL
     TPYDAENYFD YDSLNNGPSL QHWFGVDSLG RDIFSRVLVG AQISLAAGVF AVFIGAIIGT
     VLGLLAGYYE GWWDRFIMRI CDVLFAFPGI LLAIAVVAVL GSGIANVIVA VAIFSIPAFA
     RLVRGNTLVL KQQTFIESAR SIGASDTTIL FSHILPGTVS SIVVFFTMRI GTSIISAASL
     SFLGLGAQPP TPEWGAMLNE ARADMVIAPH VALFPAVAIF LTVLAFNLLG DGLRDALDPK
     IKG