ID   HISQ_SALTY              Reviewed;         228 AA.
AC   P0A2I9; P02913;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Histidine transport system permease protein HisQ;
GN   Name=hisQ; OrderedLocusNames=STM2353;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RX   PubMed=7050725; DOI=10.1038/298723a0;
RA   Higgins C.F., Haag P.D., Nikaido K., Ardeshir F., Garcia G., Ames G.F.-L.;
RT   "Complete nucleotide sequence and identification of membrane components of
RT   the histidine transport operon of S. typhimurium.";
RL   Nature 298:723-727(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [3]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=2033074; DOI=10.1016/s0021-9258(18)92898-x;
RA   Kerppola R.E., Shyamala V.K., Klebba P., Ames G.F.;
RT   "The membrane-bound proteins of periplasmic permeases form a complex.
RT   Identification of the histidine permease HisQMP complex.";
RL   J. Biol. Chem. 266:9857-9865(1991).
RN   [4]
RP   TOPOLOGY.
RX   PubMed=1733937; DOI=10.1016/s0021-9258(18)45882-6;
RA   Kerppola R.E., Ames G.F.-L.;
RT   "Topology of the hydrophobic membrane-bound components of the histidine
RT   periplasmic permease. Comparison with other members of the family.";
RL   J. Biol. Chem. 267:2329-2336(1992).
RN   [5]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=9520394; DOI=10.1073/pnas.95.7.3495;
RA   Liu P.Q., Ames G.F.;
RT   "In vitro disassembly and reassembly of an ABC transporter, the histidine
RT   permease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:3495-3500(1998).
RN   [6]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=24021237; DOI=10.1016/j.bbamem.2013.08.024;
RA   Heuveling J., Frochaux V., Ziomkowska J., Wawrzinek R., Wessig P.,
RA   Herrmann A., Schneider E.;
RT   "Conformational changes of the bacterial type I ATP-binding cassette
RT   importer HisQMP2 at distinct steps of the catalytic cycle.";
RL   Biochim. Biophys. Acta 1838:106-116(2014).
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.
CC       {ECO:0000269|PubMed:24021237, ECO:0000269|PubMed:7050725,
CC       ECO:0000269|PubMed:9520394}.
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:0000269|PubMed:2033074,
CC       ECO:0000269|PubMed:24021237, ECO:0000269|PubMed:7050725,
CC       ECO:0000269|PubMed:9520394}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2033074};
CC       Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441,
CC       ECO:0000269|PubMed:2033074}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. HisMQ subfamily. {ECO:0000305}.
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DR   EMBL; V01373; CAA24660.1; -; Genomic_DNA.
DR   EMBL; J01805; AAA75579.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL21254.1; -; Genomic_DNA.
DR   PIR; A03410; MMEBQT.
DR   RefSeq; NP_461295.1; NC_003197.2.
DR   RefSeq; WP_000965498.1; NC_003197.2.
DR   AlphaFoldDB; P0A2I9; -.
DR   SMR; P0A2I9; -.
DR   STRING; 99287.STM2353; -.
DR   TCDB; 3.A.1.3.1; the atp-binding cassette (abc) superfamily.
DR   PaxDb; P0A2I9; -.
DR   EnsemblBacteria; AAL21254; AAL21254; STM2353.
DR   GeneID; 1253875; -.
DR   KEGG; stm:STM2353; -.
DR   PATRIC; fig|99287.12.peg.2490; -.
DR   HOGENOM; CLU_019602_1_4_6; -.
DR   OMA; IWTFVWI; -.
DR   PhylomeDB; P0A2I9; -.
DR   BioCyc; SENT99287:STM2353-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..228
FT                   /note="Histidine transport system permease protein HisQ"
FT                   /id="PRO_0000060052"
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