SACC_BACSU
ID SACC_BACSU Reviewed; 677 AA.
AC P05656;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Levanase;
DE EC=3.2.1.80;
DE AltName: Full=Beta-D-fructofuranosidase;
DE AltName: Full=Exo-beta-D-fructosidase;
DE AltName: Full=Exo-levanase;
DE Flags: Precursor;
GN Name=sacC; OrderedLocusNames=BSU27030;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3112519; DOI=10.1007/bf00330439;
RA Martin I., Debarbouille M., Ferrari E., Klier A., Rapoport G.;
RT "Characterization of the levanase gene of Bacillus subtilis which shows
RT homology to yeast invertase.";
RL Mol. Gen. Genet. 208:177-184(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=3120151; DOI=10.1093/nar/15.22.9606;
RA Schoergendorfer K., Schwab H., Lafferty R.M.;
RT "Nucleotide sequence of a cloned 2.5 kb PstI-EcoRI Bacillus subtilis DNA
RT fragment coding for levanase.";
RL Nucleic Acids Res. 15:9606-9606(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9141695; DOI=10.1099/00221287-143-4-1321;
RA Parro V., San Roman M., Galindo I., Purnelle B., Bolotin A., Sorokin A.,
RA Mellado R.P.;
RT "A 23911 bp region of the Bacillus subtilis genome comprising genes located
RT upstream and downstream of the lev operon.";
RL Microbiology 143:1321-1326(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RX PubMed=2117666; DOI=10.1016/0022-2836(90)90284-s;
RA Martin-Verstraete I., Debarbouille M., Klier A., Rapoport G.;
RT "Levanase operon of Bacillus subtilis includes a fructose-specific
RT phosphotransferase system regulating the expression of the operon.";
RL J. Mol. Biol. 214:657-671(1990).
RN [6]
RP INDUCTION, AND TRANSCRIPTIONAL REGULATION.
RX PubMed=2495266; DOI=10.1128/jb.171.4.1885-1892.1989;
RA Martin I., Debarbouille M., Klier A., Rapoport G.;
RT "Induction and metabolite regulation of levanase synthesis in Bacillus
RT subtilis.";
RL J. Bacteriol. 171:1885-1892(1989).
RN [7]
RP FUNCTION, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7646030; DOI=10.1128/aem.61.5.1953-1958.1995;
RA Wanker E., Huber A., Schwab H.;
RT "Purification and characterization of the Bacillus subtilis levanase
RT produced in Escherichia coli.";
RL Appl. Environ. Microbiol. 61:1953-1958(1995).
RN [8]
RP SUBCELLULAR LOCATION, AND SECRETION PROCESS.
RX PubMed=10217495; DOI=10.1099/13500872-145-3-613;
RA Leloup L., Le Saux J., Petit-Glatron M.-F., Chambert R.;
RT "Kinetics of the secretion of Bacillus subtilis levanase overproduced
RT during the exponential phase of growth.";
RL Microbiology 145:613-619(1999).
CC -!- FUNCTION: Exo-fructosidase that can hydrolyze both levan and inulin,
CC leading to the production of free fructose. Is also able to hydrolyze
CC sucrose and to a small extent raffinose, but not melezitose,
CC stachylose, cellobiose, maltose, and lactose.
CC {ECO:0000269|PubMed:7646030}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing (2->1)- and (2->6)-linked
CC beta-D-fructofuranose residues in fructans.; EC=3.2.1.80;
CC -!- ACTIVITY REGULATION: Is completely inhibited by Ag(+) and Hg(2+) ions.
CC {ECO:0000269|PubMed:7646030}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 uM for levan (at pH 5.5 and 55 degrees Celsius)
CC {ECO:0000269|PubMed:7646030};
CC KM=6.7 mM for inulin (at pH 5.5 and 55 degrees Celsius)
CC {ECO:0000269|PubMed:7646030};
CC KM=64 mM for sucrose (at pH 5.5 and 55 degrees Celsius)
CC {ECO:0000269|PubMed:7646030};
CC pH dependence:
CC Optimum pH is 5.5 for inulin hydrolysis.
CC {ECO:0000269|PubMed:7646030};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius for inulin hydrolysis. Is
CC rapidly inactivated at 60 degrees Celsius. High stable at 50 and 55
CC degrees Celsius. {ECO:0000269|PubMed:7646030};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10217495}.
CC -!- INDUCTION: Induced by low concentrations of fructose, but not by
CC sucrose. Repressed by glucose or high concentrations of fructose.
CC {ECO:0000269|PubMed:2495266}.
CC -!- MISCELLANEOUS: Levanase cannot be detected in the wild-type B.subtilis
CC but is mostly secreted into the culture medium by SacL mutants,
CC especially at the end of the exponential growth phase.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA29137.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X05649; CAA29137.1; ALT_INIT; Genomic_DNA.
DR EMBL; Y00485; CAA68542.1; -; Genomic_DNA.
DR EMBL; X92868; CAA63465.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14645.1; -; Genomic_DNA.
DR EMBL; X56098; CAA39581.1; -; Genomic_DNA.
DR PIR; A27286; A27286.
DR RefSeq; NP_390581.1; NC_000964.3.
DR RefSeq; WP_004398804.1; NZ_JNCM01000036.1.
DR PDB; 4AZZ; X-ray; 1.70 A; A/B=515-677.
DR PDB; 4B1L; X-ray; 1.65 A; A=515-677.
DR PDB; 4B1M; X-ray; 1.10 A; A/B/C=515-677.
DR PDBsum; 4AZZ; -.
DR PDBsum; 4B1L; -.
DR PDBsum; 4B1M; -.
DR AlphaFoldDB; P05656; -.
DR SMR; P05656; -.
DR STRING; 224308.BSU27030; -.
DR CAZy; CBM66; Carbohydrate-Binding Module Family 66.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PaxDb; P05656; -.
DR PRIDE; P05656; -.
DR DNASU; 938092; -.
DR EnsemblBacteria; CAB14645; CAB14645; BSU_27030.
DR GeneID; 938092; -.
DR KEGG; bsu:BSU27030; -.
DR PATRIC; fig|224308.179.peg.2936; -.
DR eggNOG; COG1621; Bacteria.
DR InParanoid; P05656; -.
DR OMA; YYAGEYH; -.
DR PhylomeDB; P05656; -.
DR BioCyc; BSUB:BSU27030-MON; -.
DR BRENDA; 3.2.1.80; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0051669; F:fructan beta-fructosidase 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; IPR018053; Glyco_hydro_32_AS.
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.
DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..677
FT /note="Levanase"
FT /id="PRO_0000033405"
FT ACT_SITE 49
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 46..49
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 105..106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 171..172
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 658
FT /note="Q -> L (in Ref. 2; CAA68542)"
FT /evidence="ECO:0000305"
FT STRAND 529..535
FT /evidence="ECO:0007829|PDB:4B1M"
FT STRAND 538..581
FT /evidence="ECO:0007829|PDB:4B1M"
FT STRAND 585..594
FT /evidence="ECO:0007829|PDB:4B1M"
FT TURN 595..598
FT /evidence="ECO:0007829|PDB:4B1M"
FT STRAND 599..606
FT /evidence="ECO:0007829|PDB:4B1M"
FT STRAND 609..617
FT /evidence="ECO:0007829|PDB:4B1M"
FT STRAND 626..633
FT /evidence="ECO:0007829|PDB:4B1M"
FT STRAND 636..641
FT /evidence="ECO:0007829|PDB:4B1M"
FT STRAND 644..650
FT /evidence="ECO:0007829|PDB:4B1M"
FT STRAND 657..676
FT /evidence="ECO:0007829|PDB:4B1M"
SQ SEQUENCE 677 AA; 75951 MW; 80FD6B0A5EE7F525 CRC64;
MKKRLIQVMI MFTLLLTMAF SADAADSSYY DEDYRPQYHF TPEANWMNDP NGMVYYAGEY
HLFYQYHPYG LQWGPMHWGH AVSKDLVTWE HLPVALYPDE KGTIFSGSAV VDKNNTSGFQ
TGKEKPLVAI YTQDREGHQV QSIAYSNDKG RTWTKYAGNP VIPNPGKKDF RDPKVFWYEK
EKKWVMVLAA GDRILIYTSK NLKQWTYASE FGQDQGSHGG VWECPDLFEL PVDGNPNQKK
WVMQVSVGNG AVSGGSGMQY FVGDFDGTHF KNENPPNKVL WTDYGRDFYA AVSWSDIPST
DSRRLWLGWM SNWQYANDVP TSPWRSATSI PRELKLKAFT EGVRVVQTPV KELETIRGTS
KKWKNLTISP ASHNVLAGQS GDAYEINAEF KVSPGSAAEF GFKVRTGENQ FTKVGYDRRN
AKLFVDRSES GNDTFNPAFN TGKETAPLKP VNGKVKLRIF VDRSSVEVFG NDGKQVITDI
ILPDRSSKGL ELYAANGGVK VKSLTIHPLK KVWGTTPFMS NMTGWTTVNG TWADTIEGKQ
GRSDGDSFIL SSASGSDFTY ESDITIKDGN GRGAGALMFR SDKDAKNGYL ANVDAKHDLV
KFFKFENGAA SVIAEYKTPI DVNKKYHLKT EAEGDRFKIY LDDRLVIDAH DSVFSEGQFG
LNVWDATAVF QNVTKES
