Reviewed, UniProtKB/Swiss-Prot P24241 (PTIBC_ECOLI)

Names and origin

Protein names

Recommended name:
    PTS system arbutin-, cellobiose-, and salicin-specific EIIBC component
Alternative name(s):
    EIIBC-Asc
      Short name=EII-Asc
Including the following 2 domains:
    1- Recommended name:
            Arbutin-, cellobiose-, and salicin-specific phosphotransferase enzyme IIB component
              EC=2.7.1.69
        Alternative name(s):
            PTS system arbutin-, cellobiose-, and salicin-specific EIIB component
    2- Recommended name:
            Arbutin, cellobiose, and salicin permease IIC component
        Alternative name(s):
            PTS system arbutin-, cellobiose-, and salicin-specific EIIC component

Gene names

Name:	ascF
Ordered Locus Names:	b2715, JW5435

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	485 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 arbutin, cellobiose, and salicin transport.
Catalytic activity	Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.
Subcellular location	Cell inner membrane; Multi-pass membrane protein. Ref.5
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. The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.
Sequence similarities	Contains 1 PTS EIIB type-1 domain. Contains 1 PTS EIIC type-1 domain.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane
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	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane 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 – 485	485	PTS system arbutin-, cellobiose-, and salicin-specific EIIBC component		PRO_0000186498
Regions
	Transmembrane	102 – 122	21	Potential
	Transmembrane	147 – 167	21	Potential
	Transmembrane	177 – 197	21	Potential
	Transmembrane	207 – 227	21	Potential
	Transmembrane	254 – 274	21	Potential
	Transmembrane	285 – 305	21	Potential
	Transmembrane	330 – 350	21	Potential
	Transmembrane	363 – 383	21	Potential
	Transmembrane	389 – 409	21	Potential
	Transmembrane	433 – 453	21	Potential
	Domain	1 – 88	88	PTS EIIB type-1
	Domain	108 – 470	363	PTS EIIC type-1
Sites
	Active site	28	1	Phosphocysteine intermediate; for EIIB activity By similarity
Experimental info
	Sequence conflict	167 – 170	4	ASAA → HLPR in AAA69225. Ref.2
	Sequence conflict	167	1	A → Q in AAA16429. Ref.1
	Sequence conflict	311	1	R → H in AAA16429. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P24241-1 [UniParc]. Last modified October 11, 2004. Version 3. Checksum: E53627EB31B9523C	FASTA	485	51,026
	10 20 30 40 50 60 MAKNYAALAR SVIAALGGVD NISAVTHCMT RLRFVIKDDA LIDSPTLKTI PGVLGVVRSD 70 80 90 100 110 120 NQCQVIIGNT VSQAFQEVVS LLPGDMQPAQ PVGKPKLTLR RIGAGILDAL IGTMSPLIPA 130 140 150 160 170 180 IIGGSMVKLL AMILEMSGVL TKGSPTLTIL NVIGDGAFFF LPLMVAASAA IKFKTNMSLA 190 200 210 220 230 240 IAIAGVLVHP SFIELMAKAA QGEHVEFALI PVTAVKYTYT VIPALVMTWC LSYIERWVDS 250 260 270 280 290 300 ITPAVTKNFL KPMLIVLIAA PLAILLIGPI GIWIGSAISA LVYTIHGYLG WLSVAIMGAL 310 320 330 340 350 360 WPLLVMTGMH RVFTPTIIQT IAETGKEGMV MPSEIGANLS LGGSSLAVAW KTKNPELRQT 370 380 390 400 410 420 ALAAAASAIM AGISEPALYG VAIRLKRPLI ASLISGFICG AVAGMAGLAS HSMAAPGLFT 430 440 450 460 470 480 SVQFFDPANP MSIVWVFAVM ALAVVLSFIL TLLLGFEDIP VEEAAAQARK YQSVQPTVAK EVSLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence, function, activation, and evolution of the cryptic asc operon of Escherichia coli K12." Hall B.G., Xu L. Mol. Biol. Evol. 9:688-706(1992) [PubMed: 1630307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[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]	"Escherichia coli K-12: a cooperatively developed annotation snapshot -- 2005." Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R., Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T., Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H., Thomson N.R., Wishart D., Wanner B.L. Nucleic Acids Res. 34:1-9(2006) [PubMed: 16397293] [Abstract] Cited for: SEQUENCE REVISION TO 167-170.
[4]	"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.
[5]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed: 15919996] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M73326 Unassigned DNA. Translation: AAA16429.1. U29579 Genomic DNA. Translation: AAA69225.1. U00096 Genomic DNA. Translation: AAT48150.1. AP009048 Genomic DNA. Translation: BAE76792.1.
PIR	G65051.
RefSeq	AP_003282.1. YP_026182.1.
3D structure databases
HSSP	HSSP built from PDB template 1IBA based on UniProtKB P05053.
ModBase	Search...
Protein family/group databases
TCDB	4.A.1.2.3. PTS glucose-glucoside (Glc) family.
Genome annotation databases
GeneID	947154.
GenomeReviews	Gene locus JW5435 in contig AP009048_GR. Gene locus b2715 in contig U00096_GR.
KEGG	ecj:JW5435. eco:b2715.
Organism-specific databases
EchoBASE	EB0084.
EcoGene	EG10086. ascF.
CMR	Search...
Phylogenomic databases
HOGENOM	P24241.
OMA	P24241. ERWVDRI.
Enzyme and pathway databases
BioCyc	EcoCyc:ASCF-MON.
Family and domain databases
InterPro	IPR018113. PTrfase_EIIB/Cys_phospho_site. IPR001996. PTS_EIIB. IPR003352. PTS_EIIC. IPR013013. PTS_EIIC_1. IPR011535. PTS_Glc-like_IIB_component. IPR004719. PTS_IIC_glc. [Graphical view]
Gene3D	G3DSA:3.30.1360.60. PTS_EIIB. 1 hit.
Pfam	PF00367. PTS_EIIB. 1 hit. PF02378. PTS_EIIC. 1 hit. [Graphical view]
ProDom	PD001476. Ptrans_EIIB. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00826. EIIB_glc. 1 hit. TIGR00852. pts-Glc. 1 hit.
PROSITE	PS51098. PTS_EIIB_TYPE_1. 1 hit. PS01035. PTS_EIIB_TYPE_1_CYS. 1 hit. PS51103. PTS_EIIC_TYPE_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PTIBC_ECOLI

Accession

Primary (citable) accession number: P24241
Secondary accession number(s): Q2MAB4, Q46880, Q6BF64

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	October 11, 2004
Last modified:	June 16, 2009
This is version 86 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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