SACB_STRMU
ID SACB_STRMU Reviewed; 795 AA.
AC P11701;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Levansucrase;
DE EC=2.4.1.10;
DE AltName: Full=Beta-D-fructofuranosyl transferase;
DE AltName: Full=Sucrose 6-fructosyl transferase;
DE Flags: Precursor;
GN Name=ftf; Synonyms=sacB; OrderedLocusNames=SMU_2028;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GS-5;
RX PubMed=2828325; DOI=10.1128/jb.170.2.810-816.1988;
RA Shiroza T., Kuramitsu H.K.;
RT "Sequence analysis of the Streptococcus mutans fructosyltransferase gene
RT and flanking regions.";
RL J. Bacteriol. 170:810-816(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 68 family. {ECO:0000305}.
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DR EMBL; M18954; AAA88584.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN59631.1; -; Genomic_DNA.
DR PIR; B28551; B28551.
DR RefSeq; NP_722325.1; NC_004350.2.
DR RefSeq; WP_002262343.1; NC_004350.2.
DR AlphaFoldDB; P11701; -.
DR SMR; P11701; -.
DR STRING; 210007.SMU_2028; -.
DR CAZy; GH68; Glycoside Hydrolase Family 68.
DR PRIDE; P11701; -.
DR EnsemblBacteria; AAN59631; AAN59631; SMU_2028.
DR KEGG; smu:SMU_2028; -.
DR PATRIC; fig|210007.7.peg.1808; -.
DR eggNOG; COG1621; Bacteria.
DR HOGENOM; CLU_013854_0_0_9; -.
DR OMA; IWDSWPV; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050053; F:levansucrase activity; IEA:UniProtKB-EC.
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 Pfam; PF02435; Glyco_hydro_68; 1.
DR Pfam; PF19258; KxYKxGKxW_sig; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
DR TIGRFAMs; TIGR03715; KxYKxGKxW; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Reference proteome; Secreted; Signal; Transferase.
FT SIGNAL 1..34
FT CHAIN 35..795
FT /note="Levansucrase"
FT /id="PRO_0000012250"
FT REGION 42..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 246
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT ACT_SITE 499
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 399..400
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 497..499
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT BINDING 517
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT SITE 400
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT CONFLICT 69
FT /note="D -> A (in Ref. 1; AAA88584)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="K -> Q (in Ref. 1; AAA88584)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="S -> A (in Ref. 1; AAA88584)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="E -> EKD (in Ref. 1; AAA88584)"
FT /evidence="ECO:0000305"
FT CONFLICT 375..377
FT /note="GDG -> VMA (in Ref. 1; AAA88584)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="S -> P (in Ref. 1; AAA88584)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="Y -> S (in Ref. 1; AAA88584)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 795 AA; 87385 MW; 4012469148B34914 CRC64;
METKVRKKMY KKGKFWVVAT ITTAMLTGIG LSSVQADEAN STQVSSELAE RSQVQENTTA
SSSAAENQDK TEVKETPSTN PAAATVENTD QTTKVITDNA AVESKASKTK DQAATVTKTS
ASTPEVGQTN EKAKATKEAD ITTPKNTIDE YGLTEQARKI ATEAGINLSS LTQKQVEALN
KVKLTSDAQT GHQMTYQEFD KIAQTLIAQD ERYAIPYFNA KAIKNMKAAT TRDAQTGQIA
DLDVWDSWPV QDAKTGEVIN WNGYQLVVAM MGIPNTNDNH IYLLYNKYGD NNFDHWKNAG
SIFGYNETPL TQEWSGSATV NEDGSLQLFY TKVDTSDKNS NNQRLATATV NLGFDDQDVR
ILSVENDKVL TPEGGDGYHY QSYQQWRSTF TGADNIAMRD PHVIEDENGD RYLVFEASTG
TENYQGEDQI YNFTNYGGSS AYNVKSLFRF LDDQDMYNRA SWANAAIGIL KLKGDKKTPE
VDQFYTPLLS STMVSDELER PNVVKLGDKY YLFTASRLNH GSNNDAWNKA NEVVGDNVVM
LGYVSDQLTN GYKPLNNSGV VLTASVPADW RTATYSYYAV PVAGSSDTLL MTAYMTNRNE
VAGKGKNSTW APSFLIQVLP DGTTKVLAEM TQQGDWIWDE SSRTTDTVGT LDTAYLPGEN
DGYIDWNVIG GYGLKPHTPG QYQPTVPSTP IHTDDIISFE VSFDGHLVIK PVKVNNDSAG
RIDQSRNSGG SLNVAFNVYA GGNISVKPSQ KSINNTKETK KAHHVSTEKK QKKGNSFFAA
LLALFSAFCV SIGFK
