Reviewed, UniProtKB/Swiss-Prot P46318 (PTJB_BACSU)

Names and origin

Protein names

Recommended name:
    Lichenan-specific phosphotransferase enzyme IIB component
    EC=2.7.1.69
Alternative name(s):
    PTS system lichenan-specific EIIB component
    EIIB-Lic

Gene names

Name:	licB
Synonyms:	celA
Ordered Locus Names:	BSU38590

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	102 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in lichenan transport.
Catalytic activity	Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.
Subcellular location	Cytoplasm Potential.
Induction	Induced by lichenan, lichenan hydrolysate and cellobiose. Subject to carbon catabolite repression.
Domain	The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain.
Sequence similarities	Contains 1 PTS EIIB type-3 domain.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cytoplasm
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein-N(PI)-phosphohistidine-sugar phosphotransferase activity Inferred from electronic annotation. Source: EC sugar binding Inferred from electronic annotation. Source: InterPro sugar:hydrogen symporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 102	102	Lichenan-specific phosphotransferase enzyme IIB component		PRO_0000186487
Regions
	Domain	1 – 102	102	PTS EIIB type-3
Sites
	Active site	7	1	Phosphocysteine intermediate By similarity
Amino acid modifications
	Modified residue	37	1	Phosphoserine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P46318-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 169F90331BDBBE9E	FASTA	102	10,955
	10 20 30 40 50 60 MNILLVCAAG MSTSLLVSKM EKSAQEQGKD YTIWAVSGDS VQNHIDKADV LLLGPQVRYM 70 80 90 100 LPQLKKLGES KGVPVDVINT VHYGTCNGAE VLKSAEQLGH VS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of a new beta-glucoside utilization system in Bacillus subtilis." Tobisch S., Glaser P., Krueger S., Hecker M. J. Bacteriol. 179:496-506(1997) [PubMed: 8990303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"Sequencing of a 65 kb region of the Bacillus subtilis genome containing the lic and cel loci, and creation of a 177 kb contig covering the gnt-sacXY region." Yoshida K., Shindo K., Sano H., Seki S., Fujimura M., Yanai N., Miwa Y., Fujita Y. Microbiology 142:3113-3123(1996) [PubMed: 8969509] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / BGSC1A1.
[3]	"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: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis." Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M. Mol. Cell. Proteomics 6:697-707(2007) [PubMed: 17218307] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z49992 Genomic DNA. Translation: CAA90285.1. D83026 Genomic DNA. Translation: BAA11743.1. AL009126 Genomic DNA. Translation: CAB15885.1.
PIR	E69651.
RefSeq	NP_391738.1.
3D structure databases
HSSP	HSSP built from PDB template 1IIB based on UniProtKB P17409.
ModBase	Search...
Protein family/group databases
TCDB	4.A.3.2.2. PTS lactose-N,N'-diacetylchitobiose-beta-glucoside (Lac) family.
PTM databases
PhosSite	P46318.
Genome annotation databases
GeneID	937379.
GenomeReviews	Gene locus BSU38590 in contig AL009126_GR.
KEGG	bsu:BSU38590.
NMPDR	fig|224308.1.peg.3864.
Organism-specific databases
SubtiList	BG11347. licB. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P46318.
OMA	DEKNVGI.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU3855-MON.
BRENDA	2.7.1.69. 150.
Family and domain databases
InterPro	IPR014350. PTrfase_system_EIIB_3_subgr. IPR013012. PTS_EIIB_3. IPR003501. PTS_IIB_lac. [Graphical view]
Pfam	PF02302. PTS_IIB. 1 hit. [Graphical view]
TIGRFAMs	TIGR00853. pts-lac. 1 hit.
PROSITE	PS51100. PTS_EIIB_TYPE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PTJB_BACSU

Accession

Primary (citable) accession number: P46318

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 3, 2009
This is version 73 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)