LEVS_FRUSA
ID LEVS_FRUSA Reviewed; 879 AA.
AC Q70XJ9;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Levansucrase {ECO:0000303|PubMed:15735966};
DE EC=2.4.1.10 {ECO:0000269|PubMed:15735966};
DE Flags: Precursor;
GN Name=levS {ECO:0000303|PubMed:15735966};
GN Synonyms=ftfA {ECO:0000312|EMBL:CAD48195.1};
OS Fructilactobacillus sanfranciscensis (Lactobacillus sanfranciscensis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Fructilactobacillus.
OX NCBI_TaxID=1625;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RC STRAIN=TMW 1.392;
RX PubMed=15735966; DOI=10.1007/s00253-004-1773-5;
RA Tieking M., Ehrmann M.A., Vogel R.F., Ganzle M.G.;
RT "Molecular and functional characterization of a levansucrase from the
RT sourdough isolate Lactobacillus sanfranciscensis TMW 1.392.";
RL Appl. Microbiol. Biotechnol. 66:655-663(2005).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=TMW 1.392;
RX DOI=10.1007/s00217-007-0738-1;
RA Kaditzky S., Seitter M., Hertel C., Vogel R.F.;
RT "Performance of Lactobacillus sanfranciscensis TMW 1.392 and its
RT levansucrase deletion mutant in wheat dough and comparison of their impact
RT on bread quality.";
RL Eur. Food Res. Technol. 227:433-442(2008).
CC -!- FUNCTION: Fructosyltransferase that catalyzes the polymerization of the
CC fructose moiety of sucrose to produce levan polymer and the fructo-
CC oligosaccharide (FOS) 1-kestose. Also displays sucrose hydrolase
CC activity. {ECO:0000269|PubMed:15735966}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[6)-beta-D-fructofuranosyl-(2->](n) alpha-D-glucopyranoside +
CC sucrose = [6)-beta-D-fructofuranosyl-(2->](n+1) alpha-D-
CC glucopyranoside + D-glucose; Xref=Rhea:RHEA:13653, Rhea:RHEA-
CC COMP:13093, Rhea:RHEA-COMP:13094, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:17992, ChEBI:CHEBI:134464; EC=2.4.1.10;
CC Evidence={ECO:0000269|PubMed:15735966};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.1 mM for sucrose (at 28 degrees Celsius)
CC {ECO:0000269|PubMed:15735966};
CC Vmax=206 umol/min/mg enzyme for the overall activity comprising both
CC transferase and hydrolase activities (at 28 degrees Celsius)
CC {ECO:0000269|PubMed:15735966};
CC pH dependence:
CC Optimum pH is 5.4. Displays 50% of the optimal activity between pH
CC values 4.0 and 6.2. A pH above 7 leads to a complete inhibition of
CC the enzyme. {ECO:0000269|PubMed:15735966};
CC Temperature dependence:
CC Optimum temperature is 35-45 degrees Celsius.
CC {ECO:0000269|PubMed:15735966};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}.
CC -!- DISRUPTION PHENOTYPE: The wild-type strain metabolizes sucrose with
CC formation of acetate, mannitol, glucose, kestose and levan while cells
CC lacking this gene do not metabolize sucrose, do not liberate glucose
CC from sucrose, and do not form mannitol, acetate, kestose or levan.
CC Growth and acidification are lower in wheat doughs prepared with the
CC deletion mutant than in those employing the wild-type.
CC {ECO:0000269|PubMed:15735966, ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 68 family. {ECO:0000305}.
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DR EMBL; AJ508391; CAD48195.1; -; Genomic_DNA.
DR AlphaFoldDB; Q70XJ9; -.
DR SMR; Q70XJ9; -.
DR CAZy; GH68; Glycoside Hydrolase Family 68.
DR BRENDA; 2.4.1.10; 31503.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0050053; F:levansucrase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009758; P:carbohydrate utilization; IEA:InterPro.
DR CDD; cd08997; GH68; 1.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR003469; Glyco_hydro_68.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR022263; KxYKxGKxW.
DR InterPro; IPR019931; LPXTG_anchor.
DR Pfam; PF02435; Glyco_hydro_68; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF19258; KxYKxGKxW_sig; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
DR TIGRFAMs; TIGR03715; KxYKxGKxW; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW Calcium; Carbohydrate metabolism; Cell wall; Glycosyltransferase;
KW Metal-binding; Peptidoglycan-anchor; Repeat; Secreted; Signal; Transferase.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..879
FT /note="Levansucrase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431245"
FT PROPEP 845..879
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000431246"
FT REPEAT 66..81
FT /note="1"
FT /evidence="ECO:0000305|PubMed:15735966"
FT REPEAT 82..97
FT /note="2"
FT /evidence="ECO:0000305|PubMed:15735966"
FT REPEAT 98..113
FT /note="3"
FT /evidence="ECO:0000305|PubMed:15735966"
FT REPEAT 114..129
FT /note="4"
FT /evidence="ECO:0000305|PubMed:15735966"
FT REPEAT 130..145
FT /note="5"
FT /evidence="ECO:0000305|PubMed:15735966"
FT REPEAT 146..161
FT /note="6"
FT /evidence="ECO:0000305|PubMed:15735966"
FT REPEAT 162..177
FT /note="7"
FT /evidence="ECO:0000305|PubMed:15735966"
FT REGION 66..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..177
FT /note="7 X 16 AA tandem repeats of D-N-A-T-S-G-S-T-K-Q-E-S-
FT S-[IV]-A-N"
FT /evidence="ECO:0000305|PubMed:15735966"
FT REGION 743..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 841..845
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 755..787
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 312
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT ACT_SITE 565
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 358
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 382
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 460
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 465..466
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 491
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 530
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 562
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 563..565
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 583
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 701
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 703
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 708
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT SITE 466
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT MOD_RES 844
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 879 AA; 94935 MW; D8FB15CEE05E1874 CRC64;
MTKEHKKMYK AGKYWAVATL VSASILMEVG VTTHADAVEN NKYDGTANVN IDCQANVDGK
IISTDDNATS GSTKQESSIA NDNATSGSTK QESSIANDNA TSGSTKQESS IANDNATSGS
TKQESSVAND NATSGSTKQE SSVANDNATS GSTKQESSVA NDNATSGSTK QESSVANDTK
TAVVDESKNT SNTENDNSQL KQTNNEQPSA ATQANLKKLN HEAAKAVQNA KIDAGSLTDE
QINELNKINF SKSAEKGAKL TFKDLEGIGN AIVKQDPQYA VPYFNAKEIK NMPASYTVDA
QTGKMAHLDV WDSWPVQDPT GYVSNYKGYQ LVIAMMGIPN TPNGDNHIYL LYNKYGDNDF
SHWRNAGSIF GTNENNVYQE WSGSAIVNDN GTIQLFYTSN DTSDYKLNDQ RLATATLNLD
VDDNGVAIKS VDNYHILFEG DGFHYQTYDQ FANGKDRKND DYCLRDPHVV QSENGDRYLV
FEANTGMEDY QSDDQIYNWA NYGGDDAFNI KSFFKLLNNK NDRELASLAN GAIGILKLNN
DQTNPKVEEV YSPLVSTLMA SDEVERVNVV KLGDKYYLFS ATRVSRGSDR ELNAKDITIV
GDNVAMIGYV SDNLMGKYKP LNNSGVVLTA SVPANWRTAT YSYYAVPVEG HPDQVLITSY
MSNKDFASGE GNYATLAPSF IVQINPDDTT TVLARATNQG DWVWDDSSRN DNMLGVLKEG
AVNSAALPGE WGKPVDWSLI NRSSGLGLKP HQPVNPSQPT TPATPVNPSQ PTTPATPVNP
SQPTTPATPV NPSATTTPAT PVNPSATTTP AKPVNPSQPT TPAKPVQAGQ ATATNFVDQR
LPQTGENNSQ SQTMSFIGIL LAMFGSLLGF LGIKKRRND
