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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
 
 
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