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HISQ_SALTI
ID   HISQ_SALTI              Reviewed;         228 AA.
AC   P0A2J0; P02913;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Histidine transport system permease protein HisQ;
GN   Name=hisQ; OrderedLocusNames=STY2583, t0511;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- FUNCTION: Part of the histidine permease ABC transporter. Also part of
CC       a lysine/arginine/ornithine transporter. Probably responsible for the
CC       translocation of the substrate across the membrane. Required to relay
CC       the ATPase-inducing signal from the solute-binding protein to HisP (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (HisP),
CC       two transmembrane proteins (HisM and HisQ) and a solute-binding protein
CC       (HisJ or ArgT). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. HisMQ subfamily. {ECO:0000305}.
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DR   EMBL; AL513382; CAD07585.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO68217.1; -; Genomic_DNA.
DR   RefSeq; NP_456895.1; NC_003198.1.
DR   RefSeq; WP_000965498.1; NZ_WSUR01000029.1.
DR   AlphaFoldDB; P0A2J0; -.
DR   SMR; P0A2J0; -.
DR   STRING; 220341.16503577; -.
DR   EnsemblBacteria; AAO68217; AAO68217; t0511.
DR   KEGG; stt:t0511; -.
DR   KEGG; sty:STY2583; -.
DR   PATRIC; fig|220341.7.peg.2615; -.
DR   eggNOG; COG4215; Bacteria.
DR   HOGENOM; CLU_019602_1_4_6; -.
DR   OMA; IWTFVWI; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0003333; P:amino acid transmembrane transport; IEA:InterPro.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR010065; AA_ABC_transptr_permease_3TM.
DR   InterPro; IPR030199; HisQ.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   PANTHER; PTHR30133:SF1; PTHR30133:SF1; 1.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   TIGRFAMs; TIGR01726; HEQRo_perm_3TM; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..228
FT                   /note="Histidine transport system permease protein HisQ"
FT                   /id="PRO_0000060051"
FT   TOPO_DOM        1..12
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        34..58
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        80..87
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        109..152
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        174..194
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        216..228
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          13..212
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   228 AA;  24620 MW;  806DF4D82F7BCF69 CRC64;
     MLYGFSGVIL QGAIVTLELA LSSVVLAVLI GLVGAGAKLS QNRVTGLIFE GYTTLIRGVP
     DLVLMLLIFY GLQIALNVVT DSLGIDQIDI DPMVAGIITL GFIYGAYFTE TFRGAFMAVP
     KGHIEAATAF GFTHGQTFRR IMFPAMMRYA LPGIGNNWQV ILKATALVSL LGLEDVVKAT
     QLAGKSTWEP FYFAVVCGLI YLVFTTVSNG VLLLLERRYS VGVKRADL
 
 
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