PTEB_BACSU
ID PTEB_BACSU Reviewed; 103 AA.
AC O05505; Q797E2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=PTS system oligo-beta-mannoside-specific EIIB component {ECO:0000303|PubMed:18177310};
DE AltName: Full=Glucomannan utilization protein B {ECO:0000303|PubMed:18177310};
DE AltName: Full=Oligo-beta-mannoside-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:18177310};
DE EC=2.7.1.205 {ECO:0000255|PROSITE-ProRule:PRU00423, ECO:0000305|PubMed:18177310};
GN Name=gmuB {ECO:0000303|PubMed:18177310}; Synonyms=ydhM;
GN OrderedLocusNames=BSU05810;
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 / JH642;
RX PubMed=9202461; DOI=10.1099/00221287-143-6-1861;
RA Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y.,
RA Ogasawara N.;
RT "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the
RT Bacillus subtilis chromosome.";
RL Microbiology 143:1861-1866(1997).
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 FUNCTION IN GLUCOMANNAN UTILIZATION, CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=168;
RX PubMed=18177310; DOI=10.1111/j.1574-6968.2007.01018.x;
RA Sadaie Y., Nakadate H., Fukui R., Yee L.M., Asai K.;
RT "Glucomannan utilization operon of Bacillus subtilis.";
RL FEMS Microbiol. Lett. 279:103-109(2008).
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (sugar PTS), a major carbohydrate active transport system,
CC catalyzes the phosphorylation of incoming sugar substrates
CC concomitantly with their translocation across the cell membrane. The
CC enzyme II GmuABC PTS system is involved in the transport of oligo-
CC glucomannans such as cellobiose or mannobiose.
CC {ECO:0000305|PubMed:18177310}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-cellobiose(out) + N(pros)-phospho-L-histidyl-[protein] = 6-
CC phospho-beta-D-glucosyl-(1->4)-D-glucose(in) + L-histidyl-[protein];
CC Xref=Rhea:RHEA:49292, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC ChEBI:CHEBI:17057, ChEBI:CHEBI:29979, ChEBI:CHEBI:58312,
CC ChEBI:CHEBI:64837; EC=2.7.1.205; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00423, ECO:0000305|PubMed:18177310};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by konjac glucomannan and by cellobiose and
CC mannobiose, the possible degradation products of glucomannan. Repressed
CC by glucose via the carbon catabolite repression system. Also repressed
CC by GmuR. {ECO:0000269|PubMed:18177310}.
CC -!- DOMAIN: The PTS EIIB type-3 domain is phosphorylated by phospho-EIIA on
CC a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC sugar substrate concomitantly with the sugar uptake processed by the
CC PTS EIIC type-3 domain. {ECO:0000255|PROSITE-ProRule:PRU00423}.
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DR EMBL; D88802; BAA19705.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12400.1; -; Genomic_DNA.
DR PIR; A69785; A69785.
DR RefSeq; NP_388462.1; NC_000964.3.
DR RefSeq; WP_003242472.1; NZ_JNCM01000031.1.
DR AlphaFoldDB; O05505; -.
DR SMR; O05505; -.
DR STRING; 224308.BSU05810; -.
DR TCDB; 4.A.3.2.10; the pts lactose-n,n'-diacetylchitobiose-Beta-glucoside (lac) family.
DR jPOST; O05505; -.
DR PaxDb; O05505; -.
DR PRIDE; O05505; -.
DR EnsemblBacteria; CAB12400; CAB12400; BSU_05810.
DR GeneID; 938018; -.
DR KEGG; bsu:BSU05810; -.
DR PATRIC; fig|224308.179.peg.625; -.
DR eggNOG; COG1440; Bacteria.
DR InParanoid; O05505; -.
DR OMA; IGPQMSF; -.
DR PhylomeDB; O05505; -.
DR BioCyc; BSUB:BSU05810-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0015774; P:polysaccharide transport; IEA:UniProtKB-KW.
DR InterPro; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR003501; PTS_EIIB_2/3.
DR InterPro; IPR013012; PTS_EIIB_3.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; SSF52794; 1.
DR PROSITE; PS51100; PTS_EIIB_TYPE_3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW Polysaccharide transport; Reference proteome; Sugar transport; Transferase;
KW Transport.
FT CHAIN 1..103
FT /note="PTS system oligo-beta-mannoside-specific EIIB
FT component"
FT /id="PRO_0000372434"
FT DOMAIN 1..103
FT /note="PTS EIIB type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00423"
FT ACT_SITE 8
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000305"
FT MOD_RES 8
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00423"
SQ SEQUENCE 103 AA; 11443 MW; 8D6696A3BB935761 CRC64;
MKKILLACSS GMSTSLLVTK MKEYAQSIGE EAEIWAVGQD KAKEDMRKAD AVLIGPQMSF
LKSELQKEAD QYNIQVEVID MMAYGMADGK KAYEQALSLM VNQ
