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P05655

- SACB_BACSU

UniProt

P05655 - SACB_BACSU

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Protein

Levansucrase

Gene

sacB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Sucrose + (6)-beta-D-fructofuranosyl-(2->)(n) alpha-D-glucopyranoside = glucose + (6)-beta-D-fructofuranosyl-(2->)(n+1) alpha-D-glucopyranoside.

GO - Molecular functioni

  1. levansucrase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate utilization Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciBSUB:BSU34450-MONOMER.
MetaCyc:BSU34450-MONOMER.
SABIO-RKP05655.

Protein family/group databases

CAZyiGH68. Glycoside Hydrolase Family 68.

Names & Taxonomyi

Protein namesi
Recommended name:
Levansucrase (EC:2.4.1.10)
Alternative name(s):
Beta-D-fructofuranosyl transferase
Sucrose 6-fructosyl transferase
Gene namesi
Name:sacB
Ordered Locus Names:BSU34450
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU34450. [Micado]

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Add
BLAST
Chaini30 – 473444LevansucrasePRO_0000012249Add
BLAST

Proteomic databases

PaxDbiP05655.

Expressioni

Inductioni

Induced by sucrose.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU34450.

Structurei

Secondary structure

1
473
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi43 – 453
Helixi48 – 525
Helixi54 – 574
Helixi61 – 633
Helixi70 – 723
Helixi77 – 793
Beta strandi83 – 919
Beta strandi95 – 973
Beta strandi103 – 1119
Beta strandi120 – 1278
Helixi133 – 1353
Beta strandi137 – 1426
Helixi147 – 1504
Helixi156 – 1583
Beta strandi161 – 1699
Beta strandi175 – 1839
Turni184 – 1885
Beta strandi189 – 20113
Beta strandi206 – 21813
Beta strandi222 – 2254
Helixi228 – 2347
Helixi236 – 2394
Beta strandi246 – 2538
Beta strandi256 – 26510
Beta strandi267 – 2693
Helixi274 – 2785
Helixi280 – 2823
Helixi287 – 29913
Helixi303 – 3086
Beta strandi311 – 3188
Beta strandi322 – 33312
Turni335 – 3373
Beta strandi342 – 3498
Beta strandi352 – 3609
Helixi361 – 3633
Beta strandi374 – 38310
Helixi391 – 3933
Beta strandi395 – 4006
Beta strandi404 – 4063
Beta strandi410 – 4167
Beta strandi419 – 43113
Beta strandi435 – 4384
Beta strandi441 – 4433
Beta strandi447 – 4526
Beta strandi455 – 4584

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OYGX-ray1.50A30-473[»]
1PT2X-ray2.10A30-473[»]
2VDTX-ray3.20A34-472[»]
3BYJX-ray2.10A1-473[»]
3BYKX-ray2.10A1-473[»]
3BYLX-ray2.10A1-473[»]
3BYNX-ray2.10A1-473[»]
ProteinModelPortaliP05655.
SMRiP05655. Positions 34-473.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05655.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 68 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG70950.
HOGENOMiHOG000041220.
InParanoidiP05655.
KOiK00692.
OMAiDIYMLGY.
OrthoDBiEOG6038XR.
PhylomeDBiP05655.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
InterProiIPR003469. Glyco_hydro_68.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PfamiPF02435. Glyco_hydro_68. 1 hit.
[Graphical view]
SUPFAMiSSF75005. SSF75005. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P05655-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNIKKFAKQA TVLTFTTALL AGGATQAFAK ETNQKPYKET YGISHITRHD
60 70 80 90 100
MLQIPEQQKN EKYQVPEFDS STIKNISSAK GLDVWDSWPL QNADGTVANY
110 120 130 140 150
HGYHIVFALA GDPKNADDTS IYMFYQKVGE TSIDSWKNAG RVFKDSDKFD
160 170 180 190 200
ANDSILKDQT QEWSGSATFT SDGKIRLFYT DFSGKHYGKQ TLTTAQVNVS
210 220 230 240 250
ASDSSLNING VEDYKSIFDG DGKTYQNVQQ FIDEGNYSSG DNHTLRDPHY
260 270 280 290 300
VEDKGHKYLV FEANTGTEDG YQGEESLFNK AYYGKSTSFF RQESQKLLQS
310 320 330 340 350
DKKRTAELAN GALGMIELND DYTLKKVMKP LIASNTVTDE IERANVFKMN
360 370 380 390 400
GKWYLFTDSR GSKMTIDGIT SNDIYMLGYV SNSLTGPYKP LNKTGLVLKM
410 420 430 440 450
DLDPNDVTFT YSHFAVPQAK GNNVVITSYM TNRGFYADKQ STFAPSFLLN
460 470
IKGKKTSVVK DSILEQGQLT VNK
Length:473
Mass (Da):52,971
Last modified:November 1, 1988 - v1
Checksum:i3FBF2F571B41D5B0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121V → I in AAA22724. (PubMed:6424671)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14202 Genomic DNA. Translation: AAA22725.1.
Z94043 Genomic DNA. Translation: CAB08015.1.
AL009126 Genomic DNA. Translation: CAB15450.1.
K01987 Genomic DNA. Translation: AAA22724.1.
X02730 Genomic DNA. Translation: CAA26513.1.
PIRiS07309. A25040.
RefSeqiNP_391325.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15450; CAB15450; BSU34450.
GeneIDi936413.
KEGGibsu:BSU34450.
PATRICi18978892. VBIBacSub10457_3609.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14202 Genomic DNA. Translation: AAA22725.1 .
Z94043 Genomic DNA. Translation: CAB08015.1 .
AL009126 Genomic DNA. Translation: CAB15450.1 .
K01987 Genomic DNA. Translation: AAA22724.1 .
X02730 Genomic DNA. Translation: CAA26513.1 .
PIRi S07309. A25040.
RefSeqi NP_391325.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1OYG X-ray 1.50 A 30-473 [» ]
1PT2 X-ray 2.10 A 30-473 [» ]
2VDT X-ray 3.20 A 34-472 [» ]
3BYJ X-ray 2.10 A 1-473 [» ]
3BYK X-ray 2.10 A 1-473 [» ]
3BYL X-ray 2.10 A 1-473 [» ]
3BYN X-ray 2.10 A 1-473 [» ]
ProteinModelPortali P05655.
SMRi P05655. Positions 34-473.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU34450.

Protein family/group databases

CAZyi GH68. Glycoside Hydrolase Family 68.

Proteomic databases

PaxDbi P05655.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15450 ; CAB15450 ; BSU34450 .
GeneIDi 936413.
KEGGi bsu:BSU34450.
PATRICi 18978892. VBIBacSub10457_3609.

Organism-specific databases

GenoListi BSU34450. [Micado ]

Phylogenomic databases

eggNOGi NOG70950.
HOGENOMi HOG000041220.
InParanoidi P05655.
KOi K00692.
OMAi DIYMLGY.
OrthoDBi EOG6038XR.
PhylomeDBi P05655.

Enzyme and pathway databases

BioCyci BSUB:BSU34450-MONOMER.
MetaCyc:BSU34450-MONOMER.
SABIO-RK P05655.

Miscellaneous databases

EvolutionaryTracei P05655.

Family and domain databases

Gene3Di 2.115.10.20. 1 hit.
InterProi IPR003469. Glyco_hydro_68.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view ]
Pfami PF02435. Glyco_hydro_68. 1 hit.
[Graphical view ]
SUPFAMi SSF75005. SSF75005. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence of the gene for the secreted Bacillus subtilis enzyme levansucrase and its genetic control sites."
    Steinmetz M., Le Coq D., Aymerich S., Gonzy-Treboul G., Gay P.
    Mol. Gen. Genet. 200:220-228(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. Denizot F.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  3. "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.
  4. "Characterization of the precursor form of the exocellular levansucrase from Bacillus subtilis."
    Fouet A., Arnaud M., Klier A., Rapoport G.
    Biochem. Biophys. Res. Commun. 119:795-800(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62.
    Strain: 168 / PY79.
  5. "Modulation of Bacillus subtilis levansucrase gene expression by sucrose and regulation of the steady-state mRNA level by sacU and sacQ genes."
    Shimotsu H., Henner D.J.
    J. Bacteriol. 168:380-388(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
  6. "yveB, encoding endolevanase LevB, is part of the sacB-yveB-yveA levansucrase tricistronic operon in Bacillus subtilis."
    Pereira Y., Petit-Glatron M.-F., Chambert R.
    Microbiology 147:3413-3419(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiSACB_BACSU
AccessioniPrimary (citable) accession number: P05655
Secondary accession number(s): P70984
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: October 29, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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