ID   ARTQ_ECOL6              Reviewed;         238 AA.
AC   P0AE35; P30861; P77290;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Arginine ABC transporter permease protein ArtQ;
GN   Name=artQ; OrderedLocusNames=c0995;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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 (By similarity). {ECO:0000250}.
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: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; AE014075; AAN79468.1; -; Genomic_DNA.
DR   RefSeq; WP_001001691.1; NC_004431.1.
DR   AlphaFoldDB; P0AE35; -.
DR   SMR; P0AE35; -.
DR   STRING; 199310.c0995; -.
DR   EnsemblBacteria; AAN79468; AAN79468; c0995.
DR   GeneID; 66670864; -.
DR   KEGG; ecc:c0995; -.
DR   eggNOG; COG4215; Bacteria.
DR   HOGENOM; CLU_019602_1_4_6; -.
DR   OMA; SVGPYRW; -.
DR   BioCyc; ECOL199310:C0995-MON; -.
DR   Proteomes; UP000001410; 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:0006865; P:amino acid transport; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..238
FT                   /note="Arginine ABC transporter permease protein ArtQ"
FT                   /id="PRO_0000059962"
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"
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