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O05512 (MANB1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mannan endo-1,4-beta-mannosidase
EC=3.2.1.78
Alternative name(s):
1,4-beta-D-mannan mannanohydrolase
Beta-mannanase
Glucomannan utilization protein G
Gene names
Name:gmuG
Synonyms:ydhT
Ordered Locus Names:BSU05880
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Seems to be involved in the degradation of glucomannan. Ref.5

Catalytic activity

Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.

Subcellular location

Secreted 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.5

Sequence similarities

Belongs to the glycosyl hydrolase 26 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.4
Chain27 – 362336Mannan endo-1,4-beta-mannosidase
PRO_0000360866

Experimental info

Sequence conflict1531K → N in BAA19712. Ref.1
Sequence conflict158 – 1603STV → ATA in BAA19712. Ref.1

Secondary structure

1 ................................................ 362
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O05512 [UniParc].

Last modified July 7, 2009. Version 2.
Checksum: C7E1D527AA001B14

FASTA36240,892
        10         20         30         40         50         60 
MFKKHTISLL IIFLLASAVL AKPIEAHTVS PVNPNAQQTT KTVMNWLAHL PNRTENRVLS 

        70         80         90        100        110        120 
GAFGGYSHDT FSMAEADRIR SATGQSPAIY GCDYARGWLE TANIEDSIDV SCNGDLMSYW 

       130        140        150        160        170        180 
KNGGIPQISL HLANPAFQSG HFKTPITNDQ YKKILDSSTV EGKRLNAMLS KIADGLQELE 

       190        200        210        220        230        240 
NQGVPVLFRP LHEMNGEWFW WGLTSYNQKD NERISLYKQL YKKIYHYMTD TRGLDHLIWV 

       250        260        270        280        290        300 
YSPDANRDFK TDFYPGASYV DIVGLDAYFQ DAYSINGYDQ LTALNKPFAF TEVGPQTANG 

       310        320        330        340        350        360 
SFDYSLFINA IKQKYPKTIY FLAWNDEWSA AVNKGASALY HDSWTLNKGE IWNGDSLTPI 


VE

« 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]"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract]
Cited for: SEQUENCE REVISION TO 153; 158 AND 160.
[4]"Proteome analysis of Bacillus subtilis extracellular proteins: a two-dimensional protein electrophoretic study."
Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.
Microbiology 146:65-75(2000) [PubMed: 10658653] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-37.
Strain: 168.
[5]"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: BAA19712.1.
AL009126 Genomic DNA. Translation: CAB12407.2.
PIRH69785.
RefSeqNP_388469.2. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WHKX-ray1.70A27-362[»]
3CBWX-ray1.27A/B20-362[»]
ProteinModelPortalO05512.
SMRO05512. Positions 27-362.
ModBaseSearch...

Protein family/group databases

CAZyGH26. Glycoside Hydrolase Family 26.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000001984; EBBACP00000001984; EBBACG00000001981.
GeneID938034.
GenomeReviewsGene locus BSU05880 in contig AL009126_GR.
KEGGbsu:BSU05880.
NMPDRfig|224308.1.peg.588.
PATRIC18972792. VBIBacSub10457_0617.

Organism-specific databases

GenoListBSU05880. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000002082.
HOGENOMHBG338461.
PhylomeDBO05512.
ProtClustDBCLSK886796.

Enzyme and pathway databases

BioCycBSUB:BSU05880-MONOMER.

Family and domain databases

InterProIPR022790. EndoGluc_H/Glyco_hydro_26.
IPR000805. Glyco_hydro_26.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR016714. Mannan-1_4-b-mannosidase.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
KOK01218.
PfamPF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PIRSFPIRSF018168. Mannan-1_4-beta-mannosidase. 1 hit.
PRINTSPR00739. GLHYDRLASE26.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMANB1_BACSU
AccessionPrimary (citable) accession number: O05512
Secondary accession number(s): Q797D6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: July 7, 2009
Last modified: January 25, 2012
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Bacillus subtilis

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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