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Entry version 62 (11 Dec 2019)
Sequence version 1 (05 Jul 2004)
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Protein

Levansucrase

Gene

levS

Organism
Lactobacillus sanfranciscensis (Lactobacillus sanfrancisco)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Fructosyltransferase that catalyzes the polymerization of the fructose moiety of sucrose to produce levan polymer and the fructo-oligosaccharide (FOS) 1-kestose. Also displays sucrose hydrolase activity.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=13.1 mM for sucrose (at 28 degrees Celsius)1 Publication
  1. Vmax=206 µmol/min/mg enzyme for the overall activity comprising both transferase and hydrolase activities (at 28 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 5.4. Displays 50% of the optimal activity between pH values 4.0 and 6.2. A pH above 7 leads to a complete inhibition of the enzyme.1 Publication

Temperature dependencei

Optimum temperature is 35-45 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei311SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei312NucleophileBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi358Calcium 1By similarity1
Binding sitei382SubstrateBy similarity1
Metal bindingi460Calcium 2By similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei466Transition state stabilizerBy similarity1
Metal bindingi491Calcium 2By similarity1
Metal bindingi530Calcium 2By similarity1
Metal bindingi562Calcium 2By similarity1
Active sitei565Proton donor/acceptorBy similarity1
Binding sitei583SubstrateBy similarity1
Metal bindingi701Calcium 1By similarity1
Metal bindingi703Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi708Calcium 1By similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosyltransferase, Transferase
Biological processCarbohydrate metabolism
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.1.10 2896

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH68 Glycoside Hydrolase Family 68

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Levansucrase1 Publication (EC:2.4.1.101 Publication)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:levS1 Publication
Synonyms:ftfAImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiLactobacillus sanfranciscensis (Lactobacillus sanfrancisco)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1625 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cell wall, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

The wild-type strain metabolizes sucrose with formation of acetate, mannitol, glucose, kestose and levan while cells lacking this gene do not metabolize sucrose, do not liberate glucose from sucrose, and do not form mannitol, acetate, kestose or levan. Growth and acidification are lower in wheat doughs prepared with the deletion mutant than in those employing the wild-type.2 Publications

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 37Sequence analysisAdd BLAST37
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000043124538 – 879LevansucraseSequence analysisAdd BLAST842
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000431246845 – 879Removed by sortasePROSITE-ProRule annotationAdd BLAST35

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei844Pentaglycyl murein peptidoglycan amidated threoninePROSITE-ProRule annotation1

Keywords - PTMi

Peptidoglycan-anchor

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q70XJ9

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati66 – 8111 PublicationAdd BLAST16
Repeati82 – 9721 PublicationAdd BLAST16
Repeati98 – 11331 PublicationAdd BLAST16
Repeati114 – 12941 PublicationAdd BLAST16
Repeati130 – 14551 PublicationAdd BLAST16
Repeati146 – 16161 PublicationAdd BLAST16
Repeati162 – 17771 PublicationAdd BLAST16

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni66 – 1777 X 16 AA tandem repeats of D-N-A-T-S-G-S-T-K-Q-E-S-S-[IV]-A-N1 PublicationAdd BLAST112
Regioni465 – 466Substrate bindingBy similarity2
Regioni563 – 565Substrate bindingBy similarity3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi841 – 845LPXTG sorting signalPROSITE-ProRule annotation5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi750 – 825Pro-richPROSITE-ProRule annotationAdd BLAST76

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyl hydrolase 68 family.Curated

Keywords - Domaini

Repeat, Signal

Family and domain databases

Conserved Domains Database

More...
CDDi
cd08997 GH68, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.115.10.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003469 Glyco_hydro_68
IPR023296 Glyco_hydro_beta-prop_sf
IPR019948 Gram-positive_anchor
IPR022263 KxYKxGKxW
IPR019931 LPXTG_anchor

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02435 Glyco_hydro_68, 1 hit
PF00746 Gram_pos_anchor, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF75005 SSF75005, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03715 KxYKxGKxW, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50847 GRAM_POS_ANCHORING, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q70XJ9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTKEHKKMYK AGKYWAVATL VSASILMEVG VTTHADAVEN NKYDGTANVN
60 70 80 90 100
IDCQANVDGK IISTDDNATS GSTKQESSIA NDNATSGSTK QESSIANDNA
110 120 130 140 150
TSGSTKQESS IANDNATSGS TKQESSVAND NATSGSTKQE SSVANDNATS
160 170 180 190 200
GSTKQESSVA NDNATSGSTK QESSVANDTK TAVVDESKNT SNTENDNSQL
210 220 230 240 250
KQTNNEQPSA ATQANLKKLN HEAAKAVQNA KIDAGSLTDE QINELNKINF
260 270 280 290 300
SKSAEKGAKL TFKDLEGIGN AIVKQDPQYA VPYFNAKEIK NMPASYTVDA
310 320 330 340 350
QTGKMAHLDV WDSWPVQDPT GYVSNYKGYQ LVIAMMGIPN TPNGDNHIYL
360 370 380 390 400
LYNKYGDNDF SHWRNAGSIF GTNENNVYQE WSGSAIVNDN GTIQLFYTSN
410 420 430 440 450
DTSDYKLNDQ RLATATLNLD VDDNGVAIKS VDNYHILFEG DGFHYQTYDQ
460 470 480 490 500
FANGKDRKND DYCLRDPHVV QSENGDRYLV FEANTGMEDY QSDDQIYNWA
510 520 530 540 550
NYGGDDAFNI KSFFKLLNNK NDRELASLAN GAIGILKLNN DQTNPKVEEV
560 570 580 590 600
YSPLVSTLMA SDEVERVNVV KLGDKYYLFS ATRVSRGSDR ELNAKDITIV
610 620 630 640 650
GDNVAMIGYV SDNLMGKYKP LNNSGVVLTA SVPANWRTAT YSYYAVPVEG
660 670 680 690 700
HPDQVLITSY MSNKDFASGE GNYATLAPSF IVQINPDDTT TVLARATNQG
710 720 730 740 750
DWVWDDSSRN DNMLGVLKEG AVNSAALPGE WGKPVDWSLI NRSSGLGLKP
760 770 780 790 800
HQPVNPSQPT TPATPVNPSQ PTTPATPVNP SQPTTPATPV NPSATTTPAT
810 820 830 840 850
PVNPSATTTP AKPVNPSQPT TPAKPVQAGQ ATATNFVDQR LPQTGENNSQ
860 870
SQTMSFIGIL LAMFGSLLGF LGIKKRRND
Length:879
Mass (Da):94,935
Last modified:July 5, 2004 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD8FB15CEE05E1874
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AJ508391 Genomic DNA Translation: CAD48195.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ508391 Genomic DNA Translation: CAD48195.1

3D structure databases

SMRiQ70XJ9
ModBaseiSearch...

Protein family/group databases

CAZyiGH68 Glycoside Hydrolase Family 68

Enzyme and pathway databases

BRENDAi2.4.1.10 2896

Family and domain databases

CDDicd08997 GH68, 1 hit
Gene3Di2.115.10.20, 1 hit
InterProiView protein in InterPro
IPR003469 Glyco_hydro_68
IPR023296 Glyco_hydro_beta-prop_sf
IPR019948 Gram-positive_anchor
IPR022263 KxYKxGKxW
IPR019931 LPXTG_anchor
PfamiView protein in Pfam
PF02435 Glyco_hydro_68, 1 hit
PF00746 Gram_pos_anchor, 1 hit
SUPFAMiSSF75005 SSF75005, 1 hit
TIGRFAMsiTIGR03715 KxYKxGKxW, 1 hit
PROSITEiView protein in PROSITE
PS50847 GRAM_POS_ANCHORING, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLEVS_LACSN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q70XJ9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 26, 2014
Last sequence update: July 5, 2004
Last modified: December 11, 2019
This is version 62 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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