ARTQ_SHIFL
ID ARTQ_SHIFL Reviewed; 238 AA.
AC P0AE36; P30861; P77290;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Arginine ABC transporter permease protein ArtQ;
GN Name=artQ; OrderedLocusNames=SF0816, S0858;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN42449.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16321.1; -; Genomic_DNA.
DR RefSeq; NP_706742.1; NC_004337.2.
DR RefSeq; WP_001001691.1; NZ_WPGW01000056.1.
DR AlphaFoldDB; P0AE36; -.
DR SMR; P0AE36; -.
DR STRING; 198214.SF0816; -.
DR EnsemblBacteria; AAN42449; AAN42449; SF0816.
DR EnsemblBacteria; AAP16321; AAP16321; S0858.
DR GeneID; 1023776; -.
DR GeneID; 66670864; -.
DR KEGG; sfl:SF0816; -.
DR KEGG; sfx:S0858; -.
DR PATRIC; fig|198214.7.peg.945; -.
DR HOGENOM; CLU_019602_1_4_6; -.
DR OMA; SVGPYRW; -.
DR OrthoDB; 1523519at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..238
FT /note="Arginine ABC transporter permease protein ArtQ"
FT /id="PRO_0000059963"
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
