Reviewed, UniProtKB/Swiss-Prot Q84C00 (GUB_CLOTM)

Names and origin

Protein names

Recommended name:
    Beta-glucanase
    EC=3.2.1.73
Alternative name(s):
    Endo-beta-1,3-1,4 glucanase
    1,3-1,4-beta-D-glucan 4-glucanohydrolase
    Lichenase
    Laminarinase

Gene names

Name:	licB
Synonyms:	lam1

Organism

Clostridium thermocellum

Taxonomic identifier

1515 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	334 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)

Catalytic activity	Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.
Subunit structure	May form part of a multienzyme complex (cellulosome).
Domain	A 24 residues domain is repeated twice in this enzyme as well as in other C.thermocellum cellulosome enzymes. This domain may function as the binding ligand for the SL component.
Sequence similarities	Belongs to the glycosyl hydrolase 16 family.

Ontologies

Keywords
Domain	Repeat Signal
Molecular function	Glycosidase Hydrolase
Gene Ontology (GO)
Biological process	polysaccharide catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	licheninase 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 – 27	27	Potential
	Chain	28 – 334	307	Beta-glucanase		PRO_0000011792
Regions
	Repeat	273 – 296	24	1
	Repeat	308 – 331	24	2
	Region	273 – 331	59	2 X 24 AA approximate repeats
	Compositional bias	252 – 269	18	Pro/Thr-rich (linker)
Sites
	Active site	136	1	Nucleophile By similarity
	Active site	140	1	Proton donor By similarity
Experimental info
	Sequence conflict	97	1	S → T in CAA41281. Ref.1
	Sequence conflict	97	1	S → T Ref.2
	Sequence conflict	149	1	A → V in CAA41281. Ref.1
	Sequence conflict	149	1	A → V Ref.2
	Sequence conflict	157	1	E → G in CAA41281. Ref.1
	Sequence conflict	157	1	E → G Ref.2
	Sequence conflict	218	1	K → I in CAA41281. Ref.1
	Sequence conflict	218	1	K → I Ref.2
	Sequence conflict	304 – 334	31	QSVAD…AIPSL → PQDGCGRHDRVVDSGSK in CAA41281. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q84C00-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 3079DEF1CEE5A664	FASTA	334	37,942
	10 20 30 40 50 60 MKNRVISLLM ASLLLVLSVI VAPFYKAEAA TVVNTPFVAV FSNFDSSQWE KADWANGSVF 70 80 90 100 110 120 NCVWKPSQVT FSNGKMILTL DREYGGSYPY KSGEYRSKSF FGYGYYEVRM KAAKNVGIVS 130 140 150 160 170 180 SFFTYTGPSD NNPWDEIDIE FLGKDTTKAQ FNWYKNEVGG NEYLHNLGFD ASQDFHTYGF 190 200 210 220 230 240 EWRPDYIDFY VDGKKVYRGT RNIPVTPGKI MMNLWPGKGV DEWLGRYDGR TPLQAEYEYV 250 260 270 280 290 300 KYYPNGVPQD NPTPTPTIAP STPTNPNLPL KGDVNGDGHV NSSDYSLFKR YLLRVIDRFP 310 320 330 VGDQSVADVN RDGRIDSTDL TMLKRYLIRA IPSL

References

[1]	"Nucleotide sequence of the Clostridium thermocellum laminarinase gene." Zverlov V.V., Laptev D.A., Tishkov V.I., Velikodvorskaja G.A. Biochem. Biophys. Res. Commun. 181:507-512(1991) [PubMed: 1755832] [Abstract] Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: F7.
[2]	Zverlov V.V. Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	Lv W.-P., Xu Z.-R., Li W.-F., Sun J.-Y., Xu Y.-X., Gu S.-H. Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Cloning the Clostridium thermocellum thermostable laminarinase gene in Escherichia coli; the properties of the enzyme thus produced." Zverlov V.V., Velikodvorskaja G.A. Biotechnol. Lett. 12:811-816(1990) Cited for: CHARACTERIZATION. Strain: F7.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X58392 Genomic DNA. Translation: CAA41281.1. AY225318 Genomic DNA. Translation: AAO74890.1.
PIR	JS0611.
3D structure databases
HSSP	HSSP built from PDB template 1AJK based on UniProtKB P23904.
SMR	Q84C00. Positions 33-244, 90-246, 270-331.
ModBase	Search...
Protein family/group databases
CAZy	GH16. Glycoside Hydrolase Family 16.
Enzyme and pathway databases
BRENDA	3.2.1.73. 97464.
Family and domain databases
InterPro	IPR008264. Beta_glucanase. IPR016134. Cellulos_enz_dockerin_1. IPR002105. Cellulos_enz_dockerin_1_Ca-bd. IPR008985. ConA-like_lec_gl. IPR013320. ConA-like_subgrp. IPR018242. Dockerin_1. IPR018247. EF_Hand_1_Ca_BS. IPR000757. Glyco_hydro_16. IPR008263. Glycoside_hydrolase_16_AS. [Graphical view]
Gene3D	G3DSA:1.10.1330.10. Cellulos_enz_dockerin_1. 1 hit. G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.
Pfam	PF00404. Dockerin_1. 2 hits. PF00722. Glyco_hydro_16. 1 hit. [Graphical view]
PRINTS	PR00737. GLHYDRLASE16.
PROSITE	PS00448. CLOS_CELLULOSOME_RPT. 2 hits. PS00018. EF_HAND_1. 2 hits. Uncertain. PS01034. GLYCOSYL_HYDROL_F16. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUB_CLOTM

Accession

Primary (citable) accession number: Q84C00
Secondary accession number(s): P29716, P37074

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 17, 2007
Last sequence update:	June 1, 2003
Last modified:	January 19, 2010
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)