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P05656 (SACC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. 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

Names and origin

Protein namesRecommended name:
Levanase

EC=3.2.1.80
Alternative name(s):
Beta-D-fructofuranosidase
Exo-beta-D-fructosidase
Exo-levanase
Gene names
Name:sacC
Ordered Locus Names:BSU27030
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length677 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Exo-fructosidase that can hydrolyze both levan and inulin, leading to the production of free fructose. Is also able to hydrolyze sucrose and to a small extent raffinose, but not melezitose, stachylose, cellobiose, maltose, and lactose. Ref.7

Catalytic activity

Hydrolysis of terminal, non-reducing (2->1)- and (2->6)-linked beta-D-fructofuranose residues in fructans.

Enzyme regulation

Is completely inhibited by Ag+ and Hg2+ ions. Ref.7

Subcellular location

Secreted Ref.8.

Induction

Induced by low concentrations of fructose, but not by sucrose. Repressed by glucose or high concentrations of fructose. Ref.6 Ref.7

Miscellaneous

Levanase cannot be detected in the wild-type B.subtilis but is mostly secreted into the culture medium by SacL mutants, especially at the end of the exponential growth phase.

Sequence similarities

Belongs to the glycosyl hydrolase 32 family.

Biophysicochemical properties

Kinetic parameters:

KM=1.2 µM for levan (at pH 5.5 and 55 degrees Celsius) Ref.7

KM=6.7 mM for inulin (at pH 5.5 and 55 degrees Celsius)

KM=64 mM for sucrose (at pH 5.5 and 55 degrees Celsius)

pH dependence:

Optimum pH is 5.5 for inulin hydrolysis.

Temperature dependence:

Optimum temperature is 55 degrees Celsius for inulin hydrolysis. Is rapidly inactivated at 60 degrees Celsius. High stable at 50 and 55 degrees Celsius.

Sequence caution

The sequence CAA29137.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionfructan beta-fructosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 677653Levanase
PRO_0000033405

Regions

Region46 – 494Substrate binding By similarity
Region105 – 1062Substrate binding By similarity
Region171 – 1722Substrate binding By similarity

Sites

Active site491 By similarity
Binding site651Substrate By similarity
Binding site731Substrate By similarity
Binding site2231Substrate By similarity
Binding site3131Substrate By similarity

Experimental info

Sequence conflict6581Q → L in CAA68542. Ref.2

Secondary structure

................... 677
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05656 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 80FD6B0A5EE7F525

FASTA67775,951
        10         20         30         40         50         60 
MKKRLIQVMI MFTLLLTMAF SADAADSSYY DEDYRPQYHF TPEANWMNDP NGMVYYAGEY 

        70         80         90        100        110        120 
HLFYQYHPYG LQWGPMHWGH AVSKDLVTWE HLPVALYPDE KGTIFSGSAV VDKNNTSGFQ 

       130        140        150        160        170        180 
TGKEKPLVAI YTQDREGHQV QSIAYSNDKG RTWTKYAGNP VIPNPGKKDF RDPKVFWYEK 

       190        200        210        220        230        240 
EKKWVMVLAA GDRILIYTSK NLKQWTYASE FGQDQGSHGG VWECPDLFEL PVDGNPNQKK 

       250        260        270        280        290        300 
WVMQVSVGNG AVSGGSGMQY FVGDFDGTHF KNENPPNKVL WTDYGRDFYA AVSWSDIPST 

       310        320        330        340        350        360 
DSRRLWLGWM SNWQYANDVP TSPWRSATSI PRELKLKAFT EGVRVVQTPV KELETIRGTS 

       370        380        390        400        410        420 
KKWKNLTISP ASHNVLAGQS GDAYEINAEF KVSPGSAAEF GFKVRTGENQ FTKVGYDRRN 

       430        440        450        460        470        480 
AKLFVDRSES GNDTFNPAFN TGKETAPLKP VNGKVKLRIF VDRSSVEVFG NDGKQVITDI 

       490        500        510        520        530        540 
ILPDRSSKGL ELYAANGGVK VKSLTIHPLK KVWGTTPFMS NMTGWTTVNG TWADTIEGKQ 

       550        560        570        580        590        600 
GRSDGDSFIL SSASGSDFTY ESDITIKDGN GRGAGALMFR SDKDAKNGYL ANVDAKHDLV 

       610        620        630        640        650        660 
KFFKFENGAA SVIAEYKTPI DVNKKYHLKT EAEGDRFKIY LDDRLVIDAH DSVFSEGQFG 

       670 
LNVWDATAVF QNVTKES 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the levanase gene of Bacillus subtilis which shows homology to yeast invertase."
Martin I., Debarbouille M., Ferrari E., Klier A., Rapoport G.
Mol. Gen. Genet. 208:177-184(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Nucleotide sequence of a cloned 2.5 kb PstI-EcoRI Bacillus subtilis DNA fragment coding for levanase."
Schoergendorfer K., Schwab H., Lafferty R.M.
Nucleic Acids Res. 15:9606-9606(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"A 23911 bp region of the Bacillus subtilis genome comprising genes located upstream and downstream of the lev operon."
Parro V., San Roman M., Galindo I., Purnelle B., Bolotin A., Sorokin A., Mellado R.P.
Microbiology 143:1321-1326(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[5]"Levanase operon of Bacillus subtilis includes a fructose-specific phosphotransferase system regulating the expression of the operon."
Martin-Verstraete I., Debarbouille M., Klier A., Rapoport G.
J. Mol. Biol. 214:657-671(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
[6]"Induction and metabolite regulation of levanase synthesis in Bacillus subtilis."
Martin I., Debarbouille M., Klier A., Rapoport G.
J. Bacteriol. 171:1885-1892(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, TRANSCRIPTIONAL REGULATION.
[7]"Purification and characterization of the Bacillus subtilis levanase produced in Escherichia coli."
Wanker E., Huber A., Schwab H.
Appl. Environ. Microbiol. 61:1953-1958(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[8]"Kinetics of the secretion of Bacillus subtilis levanase overproduced during the exponential phase of growth."
Leloup L., Le Saux J., Petit-Glatron M.-F., Chambert R.
Microbiology 145:613-619(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, SECRETION PROCESS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05649 Genomic DNA. Translation: CAA29137.1. Different initiation.
Y00485 Genomic DNA. Translation: CAA68542.1.
X92868 Genomic DNA. Translation: CAA63465.1.
AL009126 Genomic DNA. Translation: CAB14645.1.
X56098 Genomic DNA. Translation: CAA39581.1.
PIRA27286.
RefSeqNP_390581.1. NC_000964.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4AZZX-ray1.70A/B515-677[»]
4B1LX-ray1.65A515-677[»]
4B1MX-ray1.10A/B/C515-677[»]
ProteinModelPortalP05656.
SMRP05656. Positions 29-513.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU27030.

Protein family/group databases

CAZyGH32. Glycoside Hydrolase Family 32.

Proteomic databases

PaxDbP05656.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14645; CAB14645; BSU27030.
GeneID938092.
KEGGbsu:BSU27030.
PATRIC18977260. VBIBacSub10457_2819.

Organism-specific databases

GenoListBSU27030. [Micado]

Phylogenomic databases

eggNOGCOG1621.
HOGENOMHOG000181424.
KOK01212.
OMAMNNWQYG.
OrthoDBEOG6DJXZ4.
PhylomeDBP05656.

Enzyme and pathway databases

BioCycBSUB:BSU27030-MONOMER.

Family and domain databases

Gene3D2.120.10.10. 1 hit.
2.60.120.560. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR001362. Glyco_hydro_32.
IPR018053. Glyco_hydro_32_AS.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
IPR023296. Glyco_hydro_beta-prop.
IPR011040. Sialidases.
[Graphical view]
PfamPF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]
SMARTSM00640. Glyco_32. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSACC_BACSU
AccessionPrimary (citable) accession number: P05656
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: July 9, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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