HISQ_ECOLI
ID HISQ_ECOLI Reviewed; 228 AA.
AC P52094; P77635;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Histidine transport system permease protein HisQ;
GN Name=hisQ; OrderedLocusNames=b2308, JW2305;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Joshi A., Ames G.F.-L.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:15919996}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. HisMQ subfamily. {ECO:0000305}.
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DR EMBL; U47027; AAA85770.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75368.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16154.1; -; Genomic_DNA.
DR PIR; B65003; B65003.
DR RefSeq; NP_416811.1; NC_000913.3.
DR RefSeq; WP_000965522.1; NZ_LN832404.1.
DR AlphaFoldDB; P52094; -.
DR SMR; P52094; -.
DR BioGRID; 4260523; 8.
DR ComplexPortal; CPX-4328; Histidine ABC transporter complex.
DR ComplexPortal; CPX-4329; Polar amino acid ABC transporter complex.
DR DIP; DIP-9912N; -.
DR STRING; 511145.b2308; -.
DR TCDB; 3.A.1.3.29; the atp-binding cassette (abc) superfamily.
DR PaxDb; P52094; -.
DR PRIDE; P52094; -.
DR EnsemblBacteria; AAC75368; AAC75368; b2308.
DR EnsemblBacteria; BAA16154; BAA16154; BAA16154.
DR GeneID; 947235; -.
DR KEGG; ecj:JW2305; -.
DR KEGG; eco:b2308; -.
DR PATRIC; fig|1411691.4.peg.4426; -.
DR EchoBASE; EB2046; -.
DR eggNOG; COG4215; Bacteria.
DR HOGENOM; CLU_019602_1_4_6; -.
DR InParanoid; P52094; -.
DR OMA; IWTFVWI; -.
DR PhylomeDB; P52094; -.
DR BioCyc; EcoCyc:HISQ-MON; -.
DR PRO; PR:P52094; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005291; F:high-affinity L-histidine transmembrane transporter activity; TAS:EcoCyc.
DR GO; GO:0089718; P:amino acid import across plasma membrane; IC:ComplexPortal.
DR GO; GO:1903810; P:L-histidine import across plasma membrane; TAS:EcoCyc.
DR GO; GO:0089709; P:L-histidine transmembrane transport; TAS:EcoCyc.
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_0000060050"
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"
FT CONFLICT 15
FT /note="V -> C (in Ref. 1; AAA85770)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="D -> Y (in Ref. 1; AAA85770)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="I -> M (in Ref. 1; AAA85770)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="G -> C (in Ref. 1; AAA85770)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="P -> A (in Ref. 1; AAA85770)"
FT /evidence="ECO:0000305"
FT CONFLICT 137..138
FT /note="VF -> MC (in Ref. 1; AAA85770)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="V -> L (in Ref. 1; AAA85770)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 228 AA; 24649 MW; E30595A18C1B8E2C CRC64;
MLYGFSGVIL QGALVTLELA ISSVVLAVII GLIGAGGKLS QNRLSGLIFE GYTTLIRGVP
DLVLMLLIFY GLQIALNTVT EAMGVGQIDI DPMVAGIITL GFIYGAYFTE TFRGAFMAVP
KGHIEAATAF GFTRGQVFRR IMFPSMMRYA LPGIGNNWQV ILKSTALVSL LGLEDVVKAT
QLAGKSTWEP FYFAIVCGVI YLVFTTVSNG VLLFLERRYS VGVKRADL
