SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P05656

- SACC_BACSU

UniProt

P05656 - SACC_BACSU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Levanase

Gene
sacC, BSU27030
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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)
  3. KM=64 mM for sucrose (at pH 5.5 and 55 degrees Celsius)

pH dependencei

Optimum pH is 5.5 for inulin hydrolysis.

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei49 – 491 By similarity
Binding sitei65 – 651Substrate By similarity
Binding sitei73 – 731Substrate By similarity
Binding sitei223 – 2231Substrate By similarity
Binding sitei313 – 3131Substrate By 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.

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: 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 – 2424 Reviewed predictionAdd
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.2 Publications

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 – 5357
Beta strandi538 – 58144
Beta strandi585 – 59410
Turni595 – 5984
Beta strandi599 – 6068
Beta strandi609 – 6179
Beta strandi626 – 6338
Beta strandi636 – 6416
Beta strandi644 – 6507
Beta strandi657 – 67620

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Family & Domainsi

Region

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

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1621.
HOGENOMiHOG000181424.
KOiK01212.
OMAiMNNWQYG.
OrthoDBiEOG6DJXZ4.
PhylomeDBiP05656.

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
2.60.120.560. 1 hit.
InterProiIPR008985. 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]
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

MKKRLIQVMI MFTLLLTMAF SADAADSSYY DEDYRPQYHF TPEANWMNDP    50
NGMVYYAGEY HLFYQYHPYG LQWGPMHWGH AVSKDLVTWE HLPVALYPDE 100
KGTIFSGSAV VDKNNTSGFQ TGKEKPLVAI YTQDREGHQV QSIAYSNDKG 150
RTWTKYAGNP VIPNPGKKDF RDPKVFWYEK EKKWVMVLAA GDRILIYTSK 200
NLKQWTYASE FGQDQGSHGG VWECPDLFEL PVDGNPNQKK WVMQVSVGNG 250
AVSGGSGMQY FVGDFDGTHF KNENPPNKVL WTDYGRDFYA AVSWSDIPST 300
DSRRLWLGWM SNWQYANDVP TSPWRSATSI PRELKLKAFT EGVRVVQTPV 350
KELETIRGTS KKWKNLTISP ASHNVLAGQS GDAYEINAEF KVSPGSAAEF 400
GFKVRTGENQ FTKVGYDRRN AKLFVDRSES GNDTFNPAFN TGKETAPLKP 450
VNGKVKLRIF VDRSSVEVFG NDGKQVITDI ILPDRSSKGL ELYAANGGVK 500
VKSLTIHPLK KVWGTTPFMS NMTGWTTVNG TWADTIEGKQ GRSDGDSFIL 550
SSASGSDFTY ESDITIKDGN GRGAGALMFR SDKDAKNGYL ANVDAKHDLV 600
KFFKFENGAA SVIAEYKTPI DVNKKYHLKT EAEGDRFKIY LDDRLVIDAH 650
DSVFSEGQFG LNVWDATAVF QNVTKES 677
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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti658 – 6581Q → L in CAA68542. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi A27286.
RefSeqi NP_390581.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4AZZ X-ray 1.70 A/B 515-677 [» ]
4B1L X-ray 1.65 A 515-677 [» ]
4B1M X-ray 1.10 A/B/C 515-677 [» ]
ProteinModelPortali P05656.
SMRi P05656. Positions 29-513.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU27030.

Protein family/group databases

CAZyi GH32. Glycoside Hydrolase Family 32.

Proteomic databases

PaxDbi P05656.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB14645 ; CAB14645 ; BSU27030 .
GeneIDi 938092.
KEGGi bsu:BSU27030.
PATRICi 18977260. VBIBacSub10457_2819.

Organism-specific databases

GenoListi BSU27030. [Micado ]

Phylogenomic databases

eggNOGi COG1621.
HOGENOMi HOG000181424.
KOi K01212.
OMAi MNNWQYG.
OrthoDBi EOG6DJXZ4.
PhylomeDBi P05656.

Enzyme and pathway databases

BioCyci BSUB:BSU27030-MONOMER.

Family and domain databases

Gene3Di 2.120.10.10. 1 hit.
2.60.120.560. 1 hit.
InterProi IPR008985. 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 ]
Pfami PF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
[Graphical view ]
SMARTi SM00640. Glyco_32. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEi PS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 9, 2014
This is version 112 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