ID   D2TH53_CITRI            Unreviewed;       228 AA.
AC   D2TH53;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   04-NOV-2026, entry version 92.
DE   RecName: Full=Histidine/lysine/arginine/ornithine transport system permease protein HisQ {ECO:0000256|ARBA:ARBA00068333};
GN   Name=hisQ {ECO:0000313|EMBL:CBG89459.1};
GN   OrderedLocusNames=ROD_27161 {ECO:0000313|EMBL:CBG89459.1};
OS   Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG89459.1, ECO:0000313|Proteomes:UP000001889};
RN   [1] {ECO:0000313|EMBL:CBG89459.1, ECO:0000313|Proteomes:UP000001889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICC168 {ECO:0000313|EMBL:CBG89459.1,
RC   ECO:0000313|Proteomes:UP000001889};
RX   PubMed=19897651; DOI=10.1128/JB.01144-09;
RA   Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA   Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA   Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT   "The Citrobacter rodentium genome sequence reveals convergent evolution
RT   with human pathogenic Escherichia coli.";
RL   J. Bacteriol. 192:525-538(2010).
CC   -!- SUBUNIT: The HisPMQJ complex is composed of two ATP-binding proteins
CC       (HisP), two transmembrane proteins (HisM and HisQ) and a solute-binding
CC       protein (HisJ). The HisPMQ-ArgT complex is composed of two ATP-binding
CC       proteins (HisP), two transmembrane proteins (HisM and HisQ) and a
CC       solute-binding protein (ArgT). {ECO:0000256|ARBA:ARBA00046835}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Cell membrane
CC       {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU363032}.
CC   -!- SIMILARITY: Belongs to the binding protein-dependent transport system
CC       permease family. HisMQ subfamily. {ECO:0000256|ARBA:ARBA00096305}.
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DR   EMBL; FN543502; CBG89459.1; -; Genomic_DNA.
DR   RefSeq; WP_012906878.1; NC_013716.1.
DR   AlphaFoldDB; D2TH53; -.
DR   STRING; 637910.ROD_27161; -.
DR   PaxDb; 637910-ROD_27161; -.
DR   KEGG; cro:ROD_27161; -.
DR   eggNOG; COG4215; Bacteria.
DR   HOGENOM; CLU_019602_1_4_6; -.
DR   OMA; AASFWVY; -.
DR   OrthoDB; 9815029at2; -.
DR   Proteomes; UP000001889; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd06261; TM_PBP2; 1.
DR   FunFam; 1.10.3720.10:FF:000020; Histidine ABC transporter permease HisQ; 1.
DR   Gene3D; 1.10.3720.10; MetI-like; 1.
DR   InterPro; IPR010065; AA_ABC_transptr_permease_3TM.
DR   InterPro; IPR051613; ABC_transp_permease_HisMQ.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   NCBIfam; TIGR01726; HEQRo_perm_3TM; 1.
DR   NCBIfam; NF011714; hisQ; 1.
DR   PANTHER; PTHR30133; CATIONIC AMINO ACID TRANSPORTER, MEMBRANE COMPONENT; 1.
DR   PANTHER; PTHR30133:SF1; HISTIDINE TRANSPORT SYSTEM PERMEASE PROTEIN HISQ; 1.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   SUPFAM; SSF161098; MetI-like; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport {ECO:0000256|ARBA:ARBA00022970};
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|PROSITE-
KW   ProRule:PRU00441}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU00441}; Reference proteome {ECO:0000313|Proteomes:UP000001889};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00441};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE-
KW   ProRule:PRU00441};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU363032}.
FT   TRANSMEM        12..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00441,
FT                   ECO:0000256|RuleBase:RU363032"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00441,
FT                   ECO:0000256|RuleBase:RU363032"
FT   TRANSMEM        90..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00441,
FT                   ECO:0000256|RuleBase:RU363032"
FT   TRANSMEM        149..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00441,
FT                   ECO:0000256|RuleBase:RU363032"
FT   TRANSMEM        191..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00441,
FT                   ECO:0000256|RuleBase:RU363032"
FT   DOMAIN          13..212
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50928"
SQ   SEQUENCE   228 AA;  24537 MW;  6357EAEB17A2C378 CRC64;
     MLYGFSGVIL QGAIVTLELA LSSVVLAVLI GLVGAGAKLS QNRVTGLIFE GYTTLIRGVP
     DLVLMLLIFY GLQIALNAVT EAMGIGQIDI DPMVAGIITL GFIYGAYFTE TFRGAFMAVP
     TGHIEAATAF GFTSSQTFRR IMFPAMMRYA LPGIGNNWQV ILKATALVSL LGLEDVVKAT
     QLAGKSTWEP FYFAVVCGVI YLIFTTVSNG VLLFLERRYS VGVKRADL
//