P05656 (SACC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Levanase
EC=3.2.1.80

Alternative name(s):
Beta-D-fructofuranosidase
Exo-beta-D-fructosidase
Exo-levanase

Gene names

Name:	sacC
Ordered Locus Names:	BSU27030

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	677 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Exo-fructosidase that can hydrolyze both levan and inulin, leading to the production of free fructose. Is also able to hydrolyze sucrose and to a small extent raffinose, but not melezitose, stachylose, cellobiose, maltose, and lactose. Ref.7
Catalytic activity	Hydrolysis of terminal, non-reducing (2->1)- and (2->6)-linked beta-D-fructofuranose residues in fructans.
Enzyme regulation	Is completely inhibited by Ag+ and Hg2+ ions. Ref.7
Subcellular location	Secreted Ref.8.
Induction	Induced by low concentrations of fructose, but not by sucrose. Repressed by glucose or high concentrations of fructose. Ref.6 Ref.7
Miscellaneous	Levanase cannot be detected in the wild-type B.subtilis but is mostly secreted into the culture medium by SacL mutants, especially at the end of the exponential growth phase.
Sequence similarities	Belongs to the glycosyl hydrolase 32 family.
Biophysicochemical properties	Kinetic parameters: KM=1.2 µM for levan (at pH 5.5 and 55 degrees Celsius) Ref.7 KM=6.7 mM for inulin (at pH 5.5 and 55 degrees Celsius) KM=64 mM for sucrose (at pH 5.5 and 55 degrees Celsius) pH dependence: Optimum pH is 5.5 for inulin hydrolysis. Temperature dependence: Optimum temperature is 55 degrees Celsius for inulin hydrolysis. Is rapidly inactivated at 60 degrees Celsius. High stable at 50 and 55 degrees Celsius.
Sequence caution	The sequence CAA29137.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	fructan beta-fructosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Potential

Chain

25 – 677

653

Levanase

PRO_0000033405

Regions

Region

46 – 49

4

Substrate binding By similarity

Region

105 – 106

2

Substrate binding By similarity

Region

171 – 172

2

Substrate binding By similarity

Sites

Active site

49

1

By similarity

Binding site

65

1

Substrate By similarity

Binding site

73

1

Substrate By similarity

Binding site

223

1

Substrate By similarity

Binding site

313

1

Substrate By similarity

Experimental info

Sequence conflict

658

1

Q → L in CAA68542. Ref.2

Secondary structure

1

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.

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.

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677

Helix Strand Turn

Details...

Beta strand

529 – 535

7

Beta strand

538 – 581

44

Beta strand

585 – 594

10

Turn

595 – 598

4

Beta strand

599 – 606

8

Beta strand

609 – 617

9

Beta strand

626 – 633

8

Beta strand

636 – 641

6

Beta strand

644 – 650

7

Beta strand

657 – 676

20

Sequences

	Sequence		Length	Mass (Da)
	P05656 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 80FD6B0A5EE7F525	FASTA	677	75,951
	10 20 30 40 50 60 MKKRLIQVMI MFTLLLTMAF SADAADSSYY DEDYRPQYHF TPEANWMNDP NGMVYYAGEY 70 80 90 100 110 120 HLFYQYHPYG LQWGPMHWGH AVSKDLVTWE HLPVALYPDE KGTIFSGSAV VDKNNTSGFQ 130 140 150 160 170 180 TGKEKPLVAI YTQDREGHQV QSIAYSNDKG RTWTKYAGNP VIPNPGKKDF RDPKVFWYEK 190 200 210 220 230 240 EKKWVMVLAA GDRILIYTSK NLKQWTYASE FGQDQGSHGG VWECPDLFEL PVDGNPNQKK 250 260 270 280 290 300 WVMQVSVGNG AVSGGSGMQY FVGDFDGTHF KNENPPNKVL WTDYGRDFYA AVSWSDIPST 310 320 330 340 350 360 DSRRLWLGWM SNWQYANDVP TSPWRSATSI PRELKLKAFT EGVRVVQTPV KELETIRGTS 370 380 390 400 410 420 KKWKNLTISP ASHNVLAGQS GDAYEINAEF KVSPGSAAEF GFKVRTGENQ FTKVGYDRRN 430 440 450 460 470 480 AKLFVDRSES GNDTFNPAFN TGKETAPLKP VNGKVKLRIF VDRSSVEVFG NDGKQVITDI 490 500 510 520 530 540 ILPDRSSKGL ELYAANGGVK VKSLTIHPLK KVWGTTPFMS NMTGWTTVNG TWADTIEGKQ 550 560 570 580 590 600 GRSDGDSFIL SSASGSDFTY ESDITIKDGN GRGAGALMFR SDKDAKNGYL ANVDAKHDLV 610 620 630 640 650 660 KFFKFENGAA SVIAEYKTPI DVNKKYHLKT EAEGDRFKIY LDDRLVIDAH DSVFSEGQFG 670 LNVWDATAVF QNVTKES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the levanase gene of Bacillus subtilis which shows homology to yeast invertase." Martin I., Debarbouille M., Ferrari E., Klier A., Rapoport G. Mol. Gen. Genet. 208:177-184(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide sequence of a cloned 2.5 kb PstI-EcoRI Bacillus subtilis DNA fragment coding for levanase." Schoergendorfer K., Schwab H., Lafferty R.M. Nucleic Acids Res. 15:9606-9606(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"A 23911 bp region of the Bacillus subtilis genome comprising genes located upstream and downstream of the lev operon." Parro V., San Roman M., Galindo I., Purnelle B., Bolotin A., Sorokin A., Mellado R.P. Microbiology 143:1321-1326(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[4]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[5]	"Levanase operon of Bacillus subtilis includes a fructose-specific phosphotransferase system regulating the expression of the operon." Martin-Verstraete I., Debarbouille M., Klier A., Rapoport G. J. Mol. Biol. 214:657-671(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
[6]	"Induction and metabolite regulation of levanase synthesis in Bacillus subtilis." Martin I., Debarbouille M., Klier A., Rapoport G. J. Bacteriol. 171:1885-1892(1989) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION, TRANSCRIPTIONAL REGULATION.
[7]	"Purification and characterization of the Bacillus subtilis levanase produced in Escherichia coli." Wanker E., Huber A., Schwab H. Appl. Environ. Microbiol. 61:1953-1958(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[8]	"Kinetics of the secretion of Bacillus subtilis levanase overproduced during the exponential phase of growth." Leloup L., Le Saux J., Petit-Glatron M.-F., Chambert R. Microbiology 145:613-619(1999) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, SECRETION PROCESS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X05649 Genomic DNA. Translation: CAA29137.1. Different initiation.
Y00485 Genomic DNA. Translation: CAA68542.1.
X92868 Genomic DNA. Translation: CAA63465.1.
AL009126 Genomic DNA. Translation: CAB14645.1.
X56098 Genomic DNA. Translation: CAA39581.1.

PIR

A27286.

RefSeq

NP_390581.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4AZZ	X-ray	1.70	A/B	515-677	[»]
4B1L	X-ray	1.65	A	515-677	[»]
4B1M	X-ray	1.10	A/B/C	515-677	[»]

ProteinModelPortal

P05656.

SMR

P05656. Positions 29-513.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU27030.

Protein family/group databases

CAZy

GH32. Glycoside Hydrolase Family 32.

Proteomic databases

PaxDb

P05656.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB14645; CAB14645; BSU27030.

GeneID

938092.

KEGG

bsu:BSU27030.

PATRIC

18977260. VBIBacSub10457_2819.

Organism-specific databases

GenoList

BSU27030. [Micado]

Phylogenomic databases

eggNOG

COG1621.

HOGENOM

HOG000181424.

KO

K01212.

OMA

EANWMND.

ProtClustDB

CLSK376321.

Enzyme and pathway databases

BioCyc

BSUB:BSU27030-MONOMER.

Family and domain databases

Gene3D

2.120.10.10. 1 hit.

InterPro

IPR008985. ConA-like_lec_gl_sf.
IPR001362. Glyco_hydro_32.
IPR018053. Glyco_hydro_32_AS.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
IPR023296. Glyco_hydro_beta-prop.
IPR011040. Sialidases.
[Graphical view]

Pfam

PF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]

SMART

SM00640. Glyco_32. 1 hit.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.
SSF75005. Glyco_hydro_43_beta-prop. 1 hit.

PROSITE

PS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SACC_BACSU

Accession

Primary (citable) accession number: P05656

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program