LEVS_LACGS
ID LEVS_LACGS Reviewed; 768 AA.
AC D3WYW0;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Levansucrase {ECO:0000303|PubMed:20075040};
DE EC=2.4.1.10 {ECO:0000269|PubMed:20075040};
DE Flags: Precursor;
GN Name=levG {ECO:0000303|PubMed:20075040};
GN Synonyms=ftf {ECO:0000303|PubMed:20075040};
OS Lactobacillus gasseri.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1596;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 19992 / DSM 20077 / CIP 103699 / JCM 1130 / KCTC 3162 / NCIMB
RC 13081 / WDCM 00103 / F164;
RX PubMed=20075040; DOI=10.1099/mic.0.036616-0;
RA Anwar M.A., Kralj S., Pique A.V., Leemhuis H., van der Maarel M.J.,
RA Dijkhuizen L.;
RT "Inulin and levan synthesis by probiotic Lactobacillus gasseri strains:
RT characterization of three novel fructansucrase enzymes and their fructan
RT products.";
RL Microbiology 156:1264-1274(2010).
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. Is also able to convert raffinose into
CC a fructan polymer and a single oligosaccharide (most likely Gal-Glc-
CC Frc-Frc) in vitro; however, L.gasseri strain DSM 20077 is unable to
CC ferment raffinose. Also displays sucrose hydrolase activity.
CC {ECO:0000269|PubMed:20075040}.
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:20075040};
CC -!- ACTIVITY REGULATION: Calcium ions are required for optimal activity,
CC but do not seem to be essential since addition of EDTA causes only a
CC 48% drop in activity. {ECO:0000269|PubMed:20075040}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 3.5-4.5. {ECO:0000269|PubMed:20075040};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius. Activity drastically
CC decreases at 60 degrees Celsius. {ECO:0000269|PubMed:20075040};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}. Cell surface {ECO:0000269|PubMed:20075040}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 68 family. {ECO:0000305}.
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DR EMBL; GU166815; ACZ67287.1; -; Genomic_DNA.
DR AlphaFoldDB; D3WYW0; -.
DR SMR; D3WYW0; -.
DR CAZy; GH68; Glycoside Hydrolase Family 68.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
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; IPR019931; LPXTG_anchor.
DR Pfam; PF02435; Glyco_hydro_68; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR SUPFAM; SSF75005; SSF75005; 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; Secreted; Signal; Transferase.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..735
FT /note="Levansucrase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431243"
FT PROPEP 736..768
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000431244"
FT REGION 57..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 732..736
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 57..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..718
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 251
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT ACT_SITE 505
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 296
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 403..404
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 429
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 502
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 503..505
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 523
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 643
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 648
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT SITE 404
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT MOD_RES 735
FT /note="Pentaglycyl murein peptidoglycan amidated alanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 768 AA; 83603 MW; 5A42E5BBA0EF5EB1 CRC64;
MLENKKHKKM SLSGKSLLMG TLSTAAIVLS ASTVNAATNT DTVDNANASQ VTTVKASASV
NKNDNSGLKE NATNDKVAGT ETNLNSSLNS GKETSSQVND SKEDSSSTQV GSTPISSAII
NNGKASSDLN QDSDNISDHF KDNNSQGQSS TSSEKTELKG KIKEIVNNSG IDVTKLTNDQ
INNLNKVNFD NDPQDGTKLT LNDLDAIGQA LIRRDPKYAV PYFNAKEIKN MDAAETKDAQ
TGKTETLEIW DSWPVQDPIT GYVSNYKGYQ LVIAMMGMPK KNDNHIYLLY NKYNDNEFSH
WRNAGSIFGY NETPDLQEWS GSAIVNKDGS VQLFYTKNDT SNGKLNDQQL ATANLKLNVD
NNGVSIASVD NDHVIFIGDG KHYQTYDQFS NGKNRNRDNY TLRDPHVVEE ENGDRYLVFE
ANTGSNNYQG EDQVYRWANY GGNDKFNVNN FLSYFGNNDD QALASVANGA LGILKLSGDQ
NNPTVKLDDV YSPLVTSLMV SDEMERPDIV KVGNKYYLFS ATRLSRGTKG EITRLANKVV
GDNVAMIGFV SDSLTHGYVP LNGSGVVLTA SVPANWRTAT YSYYAVPIEG KENQLLITAY
MTNRGEVAGK GNNSTWAPSF ILQLNPDNTT TVLAKLTNQG VWVWNGDSEN KNMIGSLEKD
SPNSAALDGE WGKFIDWDAI NSYSLKPHQP VTPNVPTTPE KPENPTTPNT PDTPRTPEVP
TTPVKKTTQS ELPKAGAKDG IAATILGAIS SMLGVIGLAG ISKRKRNN
