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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

  1. fructan beta-fructosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
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

  1. extracellular region Source: UniProtKB-SubCell
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.BSU27030.

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.
OMAiALWEMPD.
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.

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.

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.BSU27030.

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.
OMAiALWEMPD.
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(1986) [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(1986) [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(1996) [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(1996) [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(1989) [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(1988) [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(1994) [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(1998) [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: April 1, 2015
This is version 118 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.