GANQ_BACSU
ID GANQ_BACSU Reviewed; 283 AA.
AC O07011; Q795J8;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Galactooligosaccharides transport system permease protein GanQ {ECO:0000305};
GN Name=ganQ; Synonyms=yvfM; OrderedLocusNames=BSU34140;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Denizot F.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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 PUTATIVE FUNCTION.
RX PubMed=17056685; DOI=10.1128/aem.01306-06;
RA Shipkowski S., Brenchley J.E.;
RT "Bioinformatic, genetic, and biochemical evidence that some glycoside
RT hydrolase family 42 beta-galactosidases are arabinogalactan type I oligomer
RT hydrolases.";
RL Appl. Environ. Microbiol. 72:7730-7738(2006).
RN [4]
RP FUNCTION, SUBUNIT, AND INDUCTION.
RX PubMed=27501980; DOI=10.1128/jb.00468-16;
RA Watzlawick H., Morabbi Heravi K., Altenbuchner J.;
RT "Role of the ganSPQAB operon in degradation of galactan by Bacillus
RT subtilis.";
RL J. Bacteriol. 198:2887-2896(2016).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=29240795; DOI=10.1371/journal.pone.0189483;
RA Ferreira M.J., Mendes A.L., de Sa-Nogueira I.;
RT "The MsmX ATPase plays a crucial role in pectin mobilization by Bacillus
RT subtilis.";
RL PLoS ONE 12:e0189483-e0189483(2017).
CC -!- FUNCTION: Involved in galactan degradation (PubMed:27501980). Part of
CC the ABC transporter complex GanPQS involved in the uptake of
CC galactooligosaccharides (PubMed:27501980, PubMed:29240795). Responsible
CC for the translocation of the substrate across the membrane (Probable).
CC {ECO:0000269|PubMed:27501980, ECO:0000269|PubMed:29240795, ECO:0000305,
CC ECO:0000305|PubMed:17056685}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MsmX),
CC two transmembrane proteins (GanP and GanQ) and a solute-binding protein
CC (GanS). {ECO:0000269|PubMed:27501980, ECO:0000269|PubMed:29240795}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- INDUCTION: Repressed by the transcriptional regulator GanR and induced
CC by galactobiose. Also repressed by glucose.
CC {ECO:0000269|PubMed:27501980}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. {ECO:0000305}.
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DR EMBL; Z94043; CAB08007.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15419.1; -; Genomic_DNA.
DR PIR; E70038; E70038.
DR RefSeq; NP_391294.1; NC_000964.3.
DR RefSeq; WP_003228283.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O07011; -.
DR SMR; O07011; -.
DR STRING; 224308.BSU34140; -.
DR TCDB; 3.A.1.1.2; the atp-binding cassette (abc) superfamily.
DR PaxDb; O07011; -.
DR EnsemblBacteria; CAB15419; CAB15419; BSU_34140.
DR GeneID; 937991; -.
DR KEGG; bsu:BSU34140; -.
DR PATRIC; fig|224308.43.peg.3578; -.
DR eggNOG; COG3833; Bacteria.
DR InParanoid; O07011; -.
DR OMA; TAWNEFP; -.
DR PhylomeDB; O07011; -.
DR BioCyc; BSUB:BSU34140-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015423; F:ABC-type maltose transporter activity; IBA:GO_Central.
DR GO; GO:0042956; P:maltodextrin transmembrane transport; IBA:GO_Central.
DR GO; GO:0015768; P:maltose transport; IBA:GO_Central.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..283
FT /note="Galactooligosaccharides transport system permease
FT protein GanQ"
FT /id="PRO_0000382425"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 76..268
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 283 AA; 31305 MW; 168D39BCB721CE2E CRC64;
MLADMKVRRY IRLLFSYLLL AFMAVIIVYP LLWTAGASFN PGNSLISTSI IPKHPTFDHY
KELFAGKESL QYVQWYVNSM KISLFTMAGS LLCVTFTAYA FSRFRFKGRK YALTLFLLLQ
MIPQFSALIA LFVLAQILGM INSHWLLILL YIGGLIPMNT YLMKGYMDSI PMDLDESAKI
DGASSTRIFF QIILPLSKPM AAVVAMNGFT GPLGDFVLSS TILRTPESYT LPVGLFNLVN
DVMGASYTTF AAGALLISIP VAVIFIMLQK NFVSGLTAGG TKG
