GANS_BACSU
ID GANS_BACSU Reviewed; 421 AA.
AC O07009; Q795J7;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Galactooligosaccharide-binding protein {ECO:0000305};
DE AltName: Full=Cyclodextrin-binding protein;
DE Flags: Precursor;
GN Name=ganS {ECO:0000303|PubMed:27501980}; Synonyms=cycB, yvfK;
GN OrderedLocusNames=BSU34160;
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;
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 CYCLODEXTRIN-BINDING PROTEIN.
RX PubMed=11682178; DOI=10.1111/j.1574-6968.2001.tb10862.x;
RA Kamionka A., Dahl M.K.;
RT "Bacillus subtilis contains a cyclodextrin-binding protein which is part of
RT a putative ABC-transporter.";
RL FEMS Microbiol. Lett. 204:55-60(2001).
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, SUBUNIT, AND DISRUPTION PHENOTYPE.
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,
CC PubMed:29240795). Part of the ABC transporter complex GanPQS involved
CC in the uptake of galactooligosaccharides (PubMed:27501980,
CC PubMed:29240795). Binds mainly galactotetraose and galactotriose
CC (PubMed:27501980). {ECO:0000269|PubMed:27501980,
CC ECO:0000269|PubMed:29240795}.
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:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- INDUCTION: Repressed by the transcriptional regulator GanR and induced
CC by galactobiose. Also repressed by glucose.
CC {ECO:0000269|PubMed:27501980}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant displays a 2-fold increase in the
CC doubling time when galactan is the sole carbon and energy source.
CC {ECO:0000269|PubMed:29240795}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally described as a cyclodextrin-binding protein,
CC but it was shown later that it has no affinity for cyclodextrin.
CC {ECO:0000305|PubMed:11682178, ECO:0000305|PubMed:27501980}.
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DR EMBL; Z94043; CAB08005.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15421.1; -; Genomic_DNA.
DR PIR; C70038; C70038.
DR RefSeq; NP_391296.1; NC_000964.3.
DR RefSeq; WP_003228280.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O07009; -.
DR SMR; O07009; -.
DR STRING; 224308.BSU34160; -.
DR TCDB; 3.A.1.1.2; the atp-binding cassette (abc) superfamily.
DR PaxDb; O07009; -.
DR PRIDE; O07009; -.
DR DNASU; 936329; -.
DR EnsemblBacteria; CAB15421; CAB15421; BSU_34160.
DR GeneID; 936329; -.
DR KEGG; bsu:BSU34160; -.
DR PATRIC; fig|224308.179.peg.3703; -.
DR eggNOG; COG2182; Bacteria.
DR InParanoid; O07009; -.
DR OMA; NGPWAVR; -.
DR PhylomeDB; O07009; -.
DR BioCyc; BSUB:BSU34160-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central.
DR GO; GO:0015144; F:carbohydrate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:1901982; F:maltose binding; 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 InterPro; IPR006060; Maltose/Cyclodextrin-bd.
DR InterPro; IPR006059; SBP.
DR Pfam; PF13416; SBP_bac_8; 1.
DR PRINTS; PR00181; MALTOSEBP.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Signal; Sugar transport; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 23..421
FT /note="Galactooligosaccharide-binding protein"
FT /id="PRO_0000360053"
FT REGION 393..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 23
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 23
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 421 AA; 45543 MW; DD02F200B12F9576 CRC64;
MKMAKKCSVF MLCAAVSLSL AACGPKESSS AKSSSKGSEL VVWEDKEKSN GIKDAVAAFE
KEHDVKVKVV EKPYAKQIED LRMDGPAGTG PDVLTMPGDQ IGTAVTEGLL KELHVKKDVQ
SLYTDASIQS QMVDQKLYGL PKAVETTVLF YNKDLITEKE LPKTLEEWYD YSKKTADGSK
FGFLALFDQI YYAESVMSGY GGYIFGKAKD GSYNPSDIGI NNEGAVKGAA LIQKFYKDGL
FPAGIIGEQG INVLESLFTE GKAAAIISGP WNVEAFSNAG INYGITKLPK LENGKNMSSF
IGVKSYNVSA FSKNEELAQE LAVFLANEKN SKTRYEETKE VPAVKSLAND PAIMKSEAAR
AVTEQSRFSE PTPNIPEMNE IWTPADSALQ TVATGKADPK QALDQAAETA KGQIKAKHSG
K
