ID   SACC_BACL7              Reviewed;         921 AA.
AC   O31411;
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=Levanase;
DE            EC=3.2.1.65;
DE   AltName: Full=2,6-beta-D-fructan fructanohydrolase;
DE   AltName: Full=Endo-levanase;
DE   Flags: Precursor; Fragment;
OS   Bacillus sp. (strain L7).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=62626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PH DEPENDENCE, ACTIVITY
RP   REGULATION, AND SUBCELLULAR LOCATION.
RX   PubMed=9297817; DOI=10.1111/j.1574-6968.1997.tb12619.x;
RA   Miasnikov A.N.;
RT   "Characterization of a novel endo-levanase and its gene from Bacillus sp.
RT   L7.";
RL   FEMS Microbiol. Lett. 154:23-28(1997).
RN   [2]
RP   IDENTIFICATION OF FRAMESHIFT.
RX   PubMed=9675868; DOI=10.1111/j.1574-6968.1998.tb13090.x;
RA   Naumoff D.G.;
RT   "Levanase gene sequence from strain Bacillus sp. L7.";
RL   FEMS Microbiol. Lett. 164:227-228(1998).
CC   -!- FUNCTION: Catalyzes the hydrolysis of levan with endo-type specificity.
CC       The products of levan hydrolysis are a mixture of fructose and a series
CC       of fructooligosaccharides up to 12-mer, with levantriose being the
CC       major oligosaccharide obtained. Is not active towards sucrose.
CC       {ECO:0000269|PubMed:9297817}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (2->6)-beta-D-fructofuranosidic linkages
CC         in (2->6)-beta-D-fructans (levans) containing more than 3 fructose
CC         units.; EC=3.2.1.65;
CC   -!- ACTIVITY REGULATION: Is completely inhibited by low concentrations of
CC       heavy metal ions, while Ca(2+) and Mg(2+) or chelating agents such as
CC       EDTA neither inhibit nor activate the enzyme to any significant extent.
CC       {ECO:0000269|PubMed:9297817}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is about 5.5 at 50 degrees Celsius and shows an apparent
CC         shift towards higher pH values at higher temperatures.
CC         {ECO:0000269|PubMed:9297817};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9297817}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
CC   -!- CAUTION: Functional characterization has been done on a chimeric
CC       protein carrying at its C-terminus a fragment of the cloning vector
CC       instead of the levanase sequence. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA73180.1; Type=Frameshift; Note=The exact location of the frameshift is not clear.; Evidence={ECO:0000305};
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DR   EMBL; Y12619; CAA73180.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; O31411; -.
DR   SMR; O31411; -.
DR   CAZy; CBM66; Carbohydrate-Binding Module Family 66.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031219; F:levanase 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; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..>921
FT                   /note="Levanase"
FT                   /id="PRO_0000344252"
FT   ACT_SITE        412
FT                   /evidence="ECO:0000250"
FT   BINDING         409..412
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         428
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         460..461
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         539..540
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         591
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         679
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   NON_TER         921
SQ   SEQUENCE   921 AA;  101206 MW;  24B04DE96067DC44 CRC64;
     MMKWFAKLIL SLSLAVVMAA SSAAISFGAS NSSLDTHASL VTQLDSAASE AAEGKSAMIN
     ESAINSNVTG WKLHGKGRME VTGEGLRLTS DPQENVMAIS ETVADDFIYE ADVMVTDPQA
     DATLLFRSGE DGWSSYMLQL ALGAGVIRLK DASGGEGVLN VERKVEAKPG DIYHLRVKAE
     GTRLQVYWGQ QYEPVIDTEA AAHRTGRLGL HVWNGSALFQ NIRVSDMSGN TLEPISSQGL
     WQPDLKGLKG TGEDGLEAKK VFRNHEADVV LEGDLILNGQ GSAGLLFRSN AQGTEGYAAV
     LQGEGERVRV YLKKADGTIL HESRVTYPSQ RESRHHLEVK AIGERIQIFV DGYEPAAIDM
     VDTAFPSGYH GVMASSGIAY FQDVYITPYA SYYTEKYRPQ YHYSPIRGSA SDPNGLVYFE
     GEYHLFHQDG GQWAHAVSRD LIHWKRLPIA LPWNDLGHVW SGSAVADTTN ASGLFGSSGG
     KGLIAYYTSY NPDRHNGNQK IGLAYSTDRG RTWKYSEEHP VVIENPGKTG EDPGGWDFRD
     PKVVRDEANN RWVMVVSGGD HIRLFTSTNL LNWTLTDQFG YGAYIRGGVW ECPDLFQLPV
     EGSKKRKWVL MISTGANPNT QGSDAEYFIG DLTPEGKFIN DNPAGTVLKT DWGKEYYASM
     SFSDMPDGRR IMLAWMTNWD YPFSFPTTGW KGQLSIPRQV SLKETEEGIR MHQTPIEELA
     QLRSPVLTSP TARWGTSGEN LLKGITSGAY EIEAELELPP TGAASEFGFR LREGDGQRTL
     VGYRAAGSKM FVDRSASGMT DFSDLFSTLH EAPLKPEGNR IKLRILVDES SVEVFGNDGR
     VVFSDVIFPD PASRGMSFYS EGGKVKVVSL QVHALQHIWR EDEAKEPRVV MDTETLELSL
     GQTKPLFASI DNGQGKGADG I