ARTQ_ECOLI
ID ARTQ_ECOLI Reviewed; 238 AA.
AC P0AE34; P30861; P77290;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Arginine ABC transporter permease protein ArtQ;
GN Name=artQ; OrderedLocusNames=b0862, JW0846;
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 / AN387;
RX PubMed=8501075; DOI=10.1128/jb.175.11.3687-3688.1993;
RA Wissenbach U., Unden G.;
RT "Physical map location of the new artPIQMJ genes of Escherichia coli,
RT encoding a periplasmic arginine transport system.";
RL J. Bacteriol. 175:3687-3688(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
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 FUNCTION, AND SUBUNIT.
RX PubMed=8801422; DOI=10.1111/j.1365-2958.1995.mmi_17040675.x;
RA Wissenbach U., Six S., Bongaerts J., Ternes D., Steinwachs S., Unden G.;
RT "A third periplasmic transport system for L-arginine in Escherichia coli:
RT molecular characterization of the artPIQMJ genes, arginine binding and
RT transport.";
RL Mol. Microbiol. 17:675-686(1995).
RN [6]
RP 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 ABC transporter complex ArtPIQMJ involved in
CC arginine transport. Probably responsible for the translocation of the
CC substrate across the membrane. {ECO:0000269|PubMed:8801422}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (ArtP),
CC two transmembrane proteins (ArtM and ArtQ) and two solute-binding
CC proteins (ArtJ and ArtI). {ECO:0000305|PubMed:8801422}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. HisMQ subfamily. {ECO:0000305}.
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DR EMBL; X86160; CAA60103.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73949.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35576.1; -; Genomic_DNA.
DR PIR; F64824; F64824.
DR RefSeq; NP_415383.1; NC_000913.3.
DR RefSeq; WP_001001691.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P0AE34; -.
DR SMR; P0AE34; -.
DR BioGRID; 4259997; 11.
DR ComplexPortal; CPX-4318; Arginine ABC transporter complex, artI variant.
DR ComplexPortal; CPX-4319; Arginine ABC transporter complex, artJ variant.
DR DIP; DIP-48128N; -.
DR IntAct; P0AE34; 2.
DR STRING; 511145.b0862; -.
DR TCDB; 3.A.1.3.3; the atp-binding cassette (abc) superfamily.
DR jPOST; P0AE34; -.
DR PaxDb; P0AE34; -.
DR PRIDE; P0AE34; -.
DR EnsemblBacteria; AAC73949; AAC73949; b0862.
DR EnsemblBacteria; BAA35576; BAA35576; BAA35576.
DR GeneID; 66670864; -.
DR GeneID; 949046; -.
DR KEGG; ecj:JW0846; -.
DR KEGG; eco:b0862; -.
DR PATRIC; fig|1411691.4.peg.1415; -.
DR EchoBASE; EB1583; -.
DR eggNOG; COG4215; Bacteria.
DR HOGENOM; CLU_019602_1_4_6; -.
DR InParanoid; P0AE34; -.
DR OMA; SVGPYRW; -.
DR PhylomeDB; P0AE34; -.
DR BioCyc; EcoCyc:ARTQ-MON; -.
DR BioCyc; MetaCyc:ARTQ-MON; -.
DR PRO; PR:P0AE34; -.
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:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0097638; P:L-arginine import across plasma membrane; IC:ComplexPortal.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR010065; AA_ABC_transptr_permease_3TM.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
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..238
FT /note="Arginine ABC transporter permease protein ArtQ"
FT /id="PRO_0000059961"
FT TOPO_DOM 1..14
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 36..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 70..98
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 120..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 190..201
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 223..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 11..223
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT CONFLICT 156..158
FT /note="QMW -> ADV (in Ref. 1; CAA60103)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 238 AA; 26217 MW; D6262BBCC3B7C44D CRC64;
MNEFFPLASA AGMTVGLAVC ALIVGLALAM FFAVWESAKW RPVAWAGSAL VTILRGLPEI
LVVLFIYFGS SQLLLTLSDG FTINLGFVQI PVQMDIENFD VSPFLCGVIA LSLLYAAYAS
QTLRGALKAV PVGQWESGQA LGLSKSAIFF RLVMPQMWRH ALPGLGNQWL VLLKDTALVS
LISVNDLMLQ TKSIATRTQE PFTWYIVAAA IYLVITLLSQ YILKRIDLRA TRFERRPS
