Reviewed, UniProtKB/Swiss-Prot P42909 (PTPB1_ECOLI)

Names and origin

Protein names

Recommended name:
    N-acetylgalactosamine-specific phosphotransferase enzyme IIB component 1
    EC=2.7.1.69
Alternative name(s):
    PTS system N-acetylgalactosamine-specific EIIB component 1
    EIIB-Aga

Gene names

Name:	agaB
Synonyms:	yraD
Ordered Locus Names:	b3138, JW3107

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	158 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Predicted.

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 N-acetylgalactosamine transport.
Catalytic activity	Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.
Subcellular location	Cytoplasm Potential.
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-4 domain.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cytoplasm
Molecular function	Kinase Transferase
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:hydrogen symporter activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 158	158	N-acetylgalactosamine-specific phosphotransferase enzyme IIB component 1		PRO_0000186658
Regions
	Domain	1 – 158	158	PTS EIIB type-4
Sites
	Active site	17	1	Pros-phosphohistidine intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P42909-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 897BA2D5FED89159	FASTA	158	17,622
	10 20 30 40 50 60 MTSPNILLTR IDNRLVHGQV GVTWTSTIGA NLLVVVDDVV ANDDIQQKLM GITAETYGFG 70 80 90 100 110 120 IRFFTIEKTI NVIGKAAPHQ KIFLICRTPQ TVRKLVEGGI DLKDVNVGNM HFSEGKKQIS 130 140 150 SKVYVDDQDL TDLRFIKQRG VNVFIQDVPG DQKEQIPD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Pathways for the utilization of N-acetyl-galactosamine and galactosamine in Escherichia coli." Brinkkoetter A., Kloess H., Alpert C.-A., Lengeler J.W. Mol. Microbiol. 37:125-135(2000) [PubMed: 10931310] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Novel phosphotransferase genes revealed by bacterial genome sequencing: a gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in Escherichia coli." Reizer J., Ramseier T.M., Reizer A., Charbit A., Saier M.H. Jr. Microbiology 142:231-250(1996) [PubMed: 8932697] [Abstract] Cited for: DISCUSSION OF SEQUENCE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF228498 Genomic DNA. Translation: AAF81090.1. U18997 Genomic DNA. Translation: AAA57941.1. U00096 Genomic DNA. Translation: AAC76172.1. AP009048 Genomic DNA. Translation: BAE77184.1.
PIR	F65103.
RefSeq	AP_003683.1. NP_417607.1.
3D structure databases
HSSP	HSSP built from PDB template 1NRZ based on UniProtKB P37081.
ModBase	Search...
Protein family/group databases
TCDB	4.A.6.1.5. PTS mannose-fructose-sorbose (Man) family.
Genome annotation databases
GeneID	947653.
GenomeReviews	Gene locus JW3107 in contig AP009048_GR. Gene locus b3138 in contig U00096_GR.
KEGG	ecj:JW3107. eco:b3138.
Organism-specific databases
EchoBASE	EB2622.
EcoGene	EG12769. agaB.
CMR	Search...
Phylogenomic databases
HOGENOM	P42909.
OMA	P42909. NDETAND.
Enzyme and pathway databases
BioCyc	EcoCyc:AGAB-MON.
Family and domain databases
InterPro	IPR004720. PTS_IIB_sorbose-sp. IPR018455. PTS_IIB_sorbose-sp_subgr. [Graphical view]
Gene3D	G3DSA:3.40.35.10. PTS_IIB_sorb. 1 hit.
Pfam	PF03830. PTSIIB_sorb. 1 hit. [Graphical view]
ProDom	PD008332. PTSIIB_sorb. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00854. pts-sorbose. 1 hit.
PROSITE	PS51101. PTS_EIIB_TYPE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PTPB1_ECOLI

Accession

Primary (citable) accession number: P42909
Secondary accession number(s): Q2M972

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 66 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)