LEVB_BACSU
ID LEVB_BACSU Reviewed; 516 AA.
AC O07003; Q795H7;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Levanbiose-producing levanase;
DE EC=3.2.1.64;
DE AltName: Full=2,6-beta-fructan 6-levanbiohydrolase;
DE AltName: Full=Endo-levanase;
GN Name=levB; Synonyms=yveB; OrderedLocusNames=BSU34460;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Denizot F.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11739774; DOI=10.1099/00221287-147-12-3413;
RA Pereira Y., Petit-Glatron M.-F., Chambert R.;
RT "yveB, encoding endolevanase LevB, is part of the sacB-yveB-yveA
RT levansucrase tricistronic operon in Bacillus subtilis.";
RL Microbiology 147:3413-3419(2001).
RN [4]
RP FUNCTION AS A LEVANBIOSE-PRODUCING LEVANASE.
RX PubMed=15528654; DOI=10.1099/mic.0.27366-0;
RA Daguer J.-P., Geissmann T., Petit-Glatron M.-F., Chambert R.;
RT "Autogenous modulation of the Bacillus subtilis sacB-levB-yveA levansucrase
RT operon by the levB transcript.";
RL Microbiology 150:3669-3679(2004).
CC -!- FUNCTION: Catalyzes the degradation of levan mainly into levanbiose
CC (difructose). Is not active on sucrose. {ECO:0000269|PubMed:11739774,
CC ECO:0000269|PubMed:15528654}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (2->6)-beta-D-fructofuranan, to remove
CC successive disaccharide residues as levanbiose, i.e. 6-(beta-D-
CC fructofuranosyl)-D-fructose, from the end of the chain.; EC=3.2.1.64;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11739774};
CC Single-pass membrane protein {ECO:0000269|PubMed:11739774}.
CC -!- INDUCTION: Induced by sucrose. {ECO:0000269|PubMed:11739774}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR EMBL; Z94043; CAB08014.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15451.1; -; Genomic_DNA.
DR PIR; E70035; E70035.
DR RefSeq; NP_391326.1; NC_000964.3.
DR RefSeq; WP_003243729.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O07003; -.
DR SMR; O07003; -.
DR STRING; 224308.BSU34460; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PaxDb; O07003; -.
DR PRIDE; O07003; -.
DR EnsemblBacteria; CAB15451; CAB15451; BSU_34460.
DR GeneID; 938616; -.
DR KEGG; bsu:BSU34460; -.
DR PATRIC; fig|224308.179.peg.3733; -.
DR eggNOG; COG1621; Bacteria.
DR InParanoid; O07003; -.
DR OMA; GTEWRHA; -.
DR PhylomeDB; O07003; -.
DR BioCyc; BSUB:BSU34460-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033912; F:2,6-beta-fructan 6-levanbiohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004575; F:sucrose alpha-glucosidase activity; IBA:GO_Central.
DR GO; GO:0005987; P:sucrose catabolic process; IBA:GO_Central.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001362; Glyco_hydro_32.
DR InterPro; IPR013189; Glyco_hydro_32_C.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell membrane; Glycosidase; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..516
FT /note="Levanbiose-producing levanase"
FT /id="PRO_0000344254"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..516
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 58
FT /evidence="ECO:0000250"
FT BINDING 55..58
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 181..182
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 516 AA; 58979 MW; EAEC526706C40762 CRC64;
MNYIKAGKWL TVFLTFLGIL LFIDLFPKEE HDQKTKSKQK PDYRAAYHFT TPDKWKNDPQ
KPIYFDGKYH YFYLYNRDYP KGNGTEWRHA VSEDLVHWTD EGVAIPKYTN PDGDIWTGSV
VVDKENTAGF GKNALVAIVT QPSAKDKKQE QYLWYSTDKG KSFKFYSGNP VMPNPGTDDF
RDPKVIWDDQ DNKWVMVMAE GSKIGFYESD NLKDWHYTSG FFPEQAGMVE CPDLYMMRAS
DGTNKWVLGA SANGKPWGKP NTYAYWTGSF DGKEFKADQT EAQWLDYGFD WYGGVTFEDS
KSTDPLEKRY ALAWMNNWDY ANNTPTMKNG FNGTDSVIRE LRLKEQDGTY SLVSQPIEAL
EQLTVSTDEI EDQDVNGSKT LSITGDTYQL DTDLSWSELK NAGVRLRESE DQKRHIDVGI
FAEGGYAYVN RAATNQPDKS NTYVESKAPY DVNKRKVHLK ILVDKTTIEV FVGDGKTVFS
NEVFPKPEDK GITLYSDGGT ASFKNITVKH FDSIHE
