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O05505 (PTEB_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Oligo-beta-mannoside-specific phosphotransferase enzyme IIB component
EC=2.7.1.69
Alternative name(s):
Glucomannan utilization protein B
PTS system oligo-beta-mannoside-specific EIIB component
Gene names
Name:gmuB
Synonyms:ydhM
Ordered Locus Names:BSU05810
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length103 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in the transport of oligo-glucomannans such as cellobiose or mannobiose Probable. Ref.3

Catalytic activity

Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.

Subcellular location

Cytoplasm Potential.

Induction

Up-regulated by konjac glucomannan and by cellobiose and mannobiose, the possible degradation products of glucomannan. Repressed by glucose via the carbon catabolite repression system. Also repressed by gmuR. Ref.3

Domain

The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain.

Sequence similarities

Contains 1 PTS EIIB type-3 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 103103Oligo-beta-mannoside-specific phosphotransferase enzyme IIB component
PRO_0000372434

Regions

Domain1 – 103103PTS EIIB type-3

Sites

Active site81Phosphocysteine intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
O05505 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 8D6696A3BB935761

FASTA10311,443
        10         20         30         40         50         60 
MKKILLACSS GMSTSLLVTK MKEYAQSIGE EAEIWAVGQD KAKEDMRKAD AVLIGPQMSF 

        70         80         90        100 
LKSELQKEAD QYNIQVEVID MMAYGMADGK KAYEQALSLM VNQ

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the Bacillus subtilis chromosome."
Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y., Ogasawara N.
Microbiology 143:1861-1866(1997) [PubMed: 9202461] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / JH642.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Glucomannan utilization operon of Bacillus subtilis."
Sadaie Y., Nakadate H., Fukui R., Yee L.M., Asai K.
FEMS Microbiol. Lett. 279:103-109(2008) [PubMed: 18177310] [Abstract]
Cited for: INDUCTION, FUNCTION IN GLUCOMANNAN UTILIZATION.
Strain: 168.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D88802 Genomic DNA. Translation: BAA19705.1.
AL009126 Genomic DNA. Translation: CAB12400.1.
PIRA69785.
RefSeqNP_388462.1. NC_000964.3.

3D structure databases

HSSPHSSP built from PDB template 1IIB based on UniProtKB P69795.
ProteinModelPortalO05505.
SMRO05505. Positions 1-102.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000002802; EBBACP00000002802; EBBACG00000002797.
GeneID938018.
GenomeReviewsGene locus BSU05810 in contig AL009126_GR.
KEGGbsu:BSU05810.
NMPDRfig|224308.1.peg.581.
PATRIC18972778. VBIBacSub10457_0610.

Organism-specific databases

GenoListBSU05810. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000001261.
HOGENOMHBG697211.
OMAIGPQMSF.
PhylomeDBO05505.
ProtClustDBCLSK873754.

Enzyme and pathway databases

BioCycBSUB:BSU05810-MONOMER.

Family and domain databases

InterProIPR003501. PTS_EIIB_2/3.
IPR013012. PTS_EIIB_3.
[Graphical view]
KOK02760.
PfamPF02302. PTS_IIB. 1 hit.
[Graphical view]
PROSITEPS51100. PTS_EIIB_TYPE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTEB_BACSU
AccessionPrimary (citable) accession number: O05505
Secondary accession number(s): Q797E2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: July 1, 1997
Last modified: January 25, 2012
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents