ID   LEVB_GEOSE              Reviewed;         395 AA.
AC   P94469;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Levanbiose-producing levanase;
DE            EC=3.2.1.64;
DE   AltName: Full=2,6-beta-fructan 6-levanbiohydrolase;
DE   AltName: Full=Levanase;
DE   Flags: Fragment;
GN   Name=levB; Synonyms=surC, surD;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TEMPERATURE DEPENDENCE.
RC   STRAIN=ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923
RC   / NCTC 10339 / R-35646 / VKM B-510;
RX   PubMed=9349714; DOI=10.1016/s0167-4781(97)00103-6;
RA   Li Y., Triccas J.A., Ferenci T.;
RT   "A novel levansucrase-levanase gene cluster in Bacillus stearothermophilus
RT   ATCC12980.";
RL   Biochim. Biophys. Acta 1353:203-208(1997).
RN   [2]
RP   IDENTIFICATION OF FRAMESHIFTS.
RX   PubMed=10377564;
RA   Naumoff D.G.;
RT   "Homologous locus of Bacillus subtilis and Bacillus stearothermophilus
RT   genomes containing levansucrase and levanase genes.";
RL   Mol. Biol. (Mosk.) 33:207-210(1999).
CC   -!- FUNCTION: Catalyzes the degradation of levan mainly into levanbiose
CC       (difructose) (By similarity). Can also hydrolyze inulin. {ECO:0000250,
CC       ECO:0000269|PubMed:9349714}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius.
CC         {ECO:0000269|PubMed:9349714};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB97112.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U34875; AAB97112.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; P94469; -.
DR   SMR; P94469; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   PRIDE; P94469; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0033912; F:2,6-beta-fructan 6-levanbiohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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; Glycosidase; Hydrolase; Membrane; Transmembrane.
FT   CHAIN           <1..>395
FT                   /note="Levanbiose-producing levanase"
FT                   /id="PRO_0000344253"
FT   ACT_SITE        1
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   BINDING         59..60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         124..125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         395
SQ   SEQUENCE   395 AA;  45098 MW;  1ECDBAFE754F9DE3 CRC64;
     DPQKPIYFNG KYHYYYLYNR GYPKGNGTEW RHYVSDDLVH WTDEGVAIPK YTNPDGDIWT
     GSVVVDKENT AGFGKNALVA IVTQPSAKDK KQEQYLWYST DKGKSFKFYS GNPVMPNPGT
     DDFRDPKVIW DDQDNKWVMV MAEGSKIGFY ESDNLKDWHY TSGFFPEQTG MVECPDLYMM
     RASDGTNKWV LGASANGKPW GKPNTYAYWT GSFDGKEFKA DQTEAQWLDY GFDWYGGVTF
     EDSKSTDPLE KRYALAWMNN WDYANNTPTM KNGFNGTDSV IREIRLKEQD GTYSLVSQPI
     EALEQLTVST DEIEDQDVNG SKTLSITGDT YQLDTDLSWS ELKNAGVRLR ESEDQKRHID
     VGIFAEDGYA YVNRAATNQP DKSNTYVESK APYDV