GLNQ_BACSU
ID GLNQ_BACSU Reviewed; 242 AA.
AC O34677; Q798R2;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Glutamine transport ATP-binding protein GlnQ;
DE EC=7.4.2.-;
GN Name=glnQ; OrderedLocusNames=BSU27430;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7551042; DOI=10.1099/13500872-141-7-1781;
RA Rodriguez F., Grandi G.;
RT "An operon encoding a novel ABC-type transport system in Bacillus
RT subtilis.";
RL Microbiology 141:1781-1784(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP INDUCTION BY TNRA.
RX PubMed=12823818; DOI=10.1046/j.1365-2958.2003.03567.x;
RA Yoshida K., Yamaguchi H., Kinehara M., Ohki Y.-H., Nakaura Y., Fujita Y.;
RT "Identification of additional TnrA-regulated genes of Bacillus subtilis
RT associated with a TnrA box.";
RL Mol. Microbiol. 49:157-165(2003).
CC -!- FUNCTION: Part of the ABC transporter complex GlnHMPQ involved in
CC glutamine transport. Probably responsible for energy coupling to the
CC transport system (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (GlnQ),
CC two transmembrane proteins (GlnM and GlnP) and a solute-binding protein
CC (GlnH). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Positively regulated by TnrA under nitrogen-limited
CC conditions. {ECO:0000269|PubMed:12823818}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; Z69371; CAA93317.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14684.1; -; Genomic_DNA.
DR PIR; G69633; G69633.
DR RefSeq; NP_390620.1; NC_000964.3.
DR RefSeq; WP_003246180.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34677; -.
DR SMR; O34677; -.
DR STRING; 224308.BSU27430; -.
DR PaxDb; O34677; -.
DR EnsemblBacteria; CAB14684; CAB14684; BSU_27430.
DR GeneID; 937558; -.
DR KEGG; bsu:BSU27430; -.
DR PATRIC; fig|224308.179.peg.2979; -.
DR eggNOG; COG1126; Bacteria.
DR InParanoid; O34677; -.
DR OMA; EFIYIIG; -.
DR PhylomeDB; O34677; -.
DR BioCyc; BSUB:BSU27430-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015424; F:ABC-type amino acid transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR030679; ABC_ATPase_HisP-typ.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR PIRSF; PIRSF039085; ABC_ATPase_HisP; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 2: Evidence at transcript level;
KW Amino-acid transport; ATP-binding; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..242
FT /note="Glutamine transport ATP-binding protein GlnQ"
FT /id="PRO_0000376832"
FT DOMAIN 2..236
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 242 AA; 27168 MW; 18F60237D4CDD708 CRC64;
MITFQNVNKH YGDFHVLKQI NLQIEKGEVV VIIGPSGSGK STLLRCINRL ESINEGVLTV
NGTAINDRKT DINQVRQNIG MVFQHFHLYP HKTVLQNIML APVKVLRQSP EQAKETARYY
LEKVGIPDKA DAYPSQLSGG QQQRVAIARG LAMKPEVMLF DEPTSALDPE MIGEVLDVMK
TLAKEGMTMV VVTHEMGFAK EVADRIVFID EGKILEEAVP AEFYANPKEE RARLFLSRIL
NH