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Protein

Levanase

Gene

sacC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Enzyme regulationi

Is completely inhibited by Ag+ and Hg2+ ions.1 Publication

Kineticsi

  1. KM=1.2 µM for levan (at pH 5.5 and 55 degrees Celsius)1 Publication
  2. KM=6.7 mM for inulin (at pH 5.5 and 55 degrees Celsius)1 Publication
  3. KM=64 mM for sucrose (at pH 5.5 and 55 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 5.5 for inulin hydrolysis.1 Publication

    Temperature dependencei

    Optimum temperature is 55 degrees Celsius for inulin hydrolysis. Is rapidly inactivated at 60 degrees Celsius. High stable at 50 and 55 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei49 – 491PROSITE-ProRule annotation
    Binding sitei65 – 651SubstrateBy similarity
    Binding sitei73 – 731SubstrateBy similarity
    Binding sitei223 – 2231SubstrateBy similarity
    Binding sitei313 – 3131SubstrateBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Enzyme and pathway databases

    BioCyciBSUB:BSU27030-MONOMER.
    BRENDAi3.2.1.80. 658.

    Protein family/group databases

    CAZyiGH32. Glycoside Hydrolase Family 32.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Levanase (EC:3.2.1.80)
    Alternative name(s):
    Beta-D-fructofuranosidase
    Exo-beta-D-fructosidase
    Exo-levanase
    Gene namesi
    Name:sacC
    Ordered Locus Names:BSU27030
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570 Componenti: Chromosome

    Organism-specific databases

    GenoListiBSU27030. [Micado]

    Subcellular locationi

    • Secreted 1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 677653LevanasePRO_0000033405Add
    BLAST

    Proteomic databases

    PaxDbiP05656.

    Expressioni

    Inductioni

    Induced by low concentrations of fructose, but not by sucrose. Repressed by glucose or high concentrations of fructose.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100014776.

    Structurei

    Secondary structure

    1
    677
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi529 – 5357Combined sources
    Beta strandi538 – 58144Combined sources
    Beta strandi585 – 59410Combined sources
    Turni595 – 5984Combined sources
    Beta strandi599 – 6068Combined sources
    Beta strandi609 – 6179Combined sources
    Beta strandi626 – 6338Combined sources
    Beta strandi636 – 6416Combined sources
    Beta strandi644 – 6507Combined sources
    Beta strandi657 – 67620Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4AZZX-ray1.70A/B515-677[»]
    4B1LX-ray1.65A515-677[»]
    4B1MX-ray1.10A/B/C515-677[»]
    ProteinModelPortaliP05656.
    SMRiP05656. Positions 29-513.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni46 – 494Substrate bindingBy similarity
    Regioni105 – 1062Substrate bindingBy similarity
    Regioni171 – 1722Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 32 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1621.
    HOGENOMiHOG000181424.
    InParanoidiP05656.
    KOiK03332.
    OMAiIQCMAYS.
    OrthoDBiEOG6DJXZ4.
    PhylomeDBiP05656.

    Family and domain databases

    Gene3Di2.120.10.10. 1 hit.
    2.60.120.560. 1 hit.
    InterProiIPR013320. ConA-like_dom.
    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]
    PfamiPF08244. Glyco_hydro_32C. 1 hit.
    PF00251. Glyco_hydro_32N. 1 hit.
    [Graphical view]
    SMARTiSM00640. Glyco_32. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    SSF75005. SSF75005. 1 hit.
    PROSITEiPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P05656-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKKRLIQVMI MFTLLLTMAF SADAADSSYY DEDYRPQYHF TPEANWMNDP
    60 70 80 90 100
    NGMVYYAGEY HLFYQYHPYG LQWGPMHWGH AVSKDLVTWE HLPVALYPDE
    110 120 130 140 150
    KGTIFSGSAV VDKNNTSGFQ TGKEKPLVAI YTQDREGHQV QSIAYSNDKG
    160 170 180 190 200
    RTWTKYAGNP VIPNPGKKDF RDPKVFWYEK EKKWVMVLAA GDRILIYTSK
    210 220 230 240 250
    NLKQWTYASE FGQDQGSHGG VWECPDLFEL PVDGNPNQKK WVMQVSVGNG
    260 270 280 290 300
    AVSGGSGMQY FVGDFDGTHF KNENPPNKVL WTDYGRDFYA AVSWSDIPST
    310 320 330 340 350
    DSRRLWLGWM SNWQYANDVP TSPWRSATSI PRELKLKAFT EGVRVVQTPV
    360 370 380 390 400
    KELETIRGTS KKWKNLTISP ASHNVLAGQS GDAYEINAEF KVSPGSAAEF
    410 420 430 440 450
    GFKVRTGENQ FTKVGYDRRN AKLFVDRSES GNDTFNPAFN TGKETAPLKP
    460 470 480 490 500
    VNGKVKLRIF VDRSSVEVFG NDGKQVITDI ILPDRSSKGL ELYAANGGVK
    510 520 530 540 550
    VKSLTIHPLK KVWGTTPFMS NMTGWTTVNG TWADTIEGKQ GRSDGDSFIL
    560 570 580 590 600
    SSASGSDFTY ESDITIKDGN GRGAGALMFR SDKDAKNGYL ANVDAKHDLV
    610 620 630 640 650
    KFFKFENGAA SVIAEYKTPI DVNKKYHLKT EAEGDRFKIY LDDRLVIDAH
    660 670
    DSVFSEGQFG LNVWDATAVF QNVTKES
    Length:677
    Mass (Da):75,951
    Last modified:November 1, 1988 - v1
    Checksum:i80FD6B0A5EE7F525
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti658 – 6581Q → L in CAA68542 (PubMed:3120151).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    PIRiA27286.
    RefSeqiNP_390581.1. NC_000964.3.
    WP_004398804.1. NZ_JNCM01000036.1.

    Genome annotation databases

    EnsemblBacteriaiCAB14645; CAB14645; BSU27030.
    GeneIDi938092.
    KEGGibsu:BSU27030.
    PATRICi18977260. VBIBacSub10457_2819.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    PIRiA27286.
    RefSeqiNP_390581.1. NC_000964.3.
    WP_004398804.1. NZ_JNCM01000036.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4AZZX-ray1.70A/B515-677[»]
    4B1LX-ray1.65A515-677[»]
    4B1MX-ray1.10A/B/C515-677[»]
    ProteinModelPortaliP05656.
    SMRiP05656. Positions 29-513.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100014776.

    Protein family/group databases

    CAZyiGH32. Glycoside Hydrolase Family 32.

    Proteomic databases

    PaxDbiP05656.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB14645; CAB14645; BSU27030.
    GeneIDi938092.
    KEGGibsu:BSU27030.
    PATRICi18977260. VBIBacSub10457_2819.

    Organism-specific databases

    GenoListiBSU27030. [Micado]

    Phylogenomic databases

    eggNOGiCOG1621.
    HOGENOMiHOG000181424.
    InParanoidiP05656.
    KOiK03332.
    OMAiIQCMAYS.
    OrthoDBiEOG6DJXZ4.
    PhylomeDBiP05656.

    Enzyme and pathway databases

    BioCyciBSUB:BSU27030-MONOMER.
    BRENDAi3.2.1.80. 658.

    Family and domain databases

    Gene3Di2.120.10.10. 1 hit.
    2.60.120.560. 1 hit.
    InterProiIPR013320. ConA-like_dom.
    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]
    PfamiPF08244. Glyco_hydro_32C. 1 hit.
    PF00251. Glyco_hydro_32N. 1 hit.
    [Graphical view]
    SMARTiSM00640. Glyco_32. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    SSF75005. SSF75005. 1 hit.
    PROSITEiPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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.
      , 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.

    Entry informationi

    Entry nameiSACC_BACSU
    AccessioniPrimary (citable) accession number: P05656
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1988
    Last modified: July 22, 2015
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.