PTS system mannose-specific EIIAB component - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P69797 (PTNAB_ECOLI)

Last modified June 16, 2009. Version 54. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    PTS system mannose-specific EIIAB component
Alternative name(s):
    EIIAB-Man
Including the following 2 domains:
    1- Recommended name:
            Mannose-specific phosphotransferase enzyme IIA component
              EC=2.7.1.-
        Alternative name(s):
            PTS system mannose-specific EIIA component
            EIII-Man
    2- Recommended name:
            Mannose-specific phosphotransferase enzyme IIB component
              EC=2.7.1.69
        Alternative name(s):
            PTS system mannose-specific EIIB component

Gene names

Name:	manX
Synonyms:	gptB, ptsL
Ordered Locus Names:	b1817, JW1806

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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 mannose transport.
Catalytic activity	Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine. Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.
Subcellular location	Cytoplasm. Cell inner membrane; Peripheral membrane protein. Ref.7
Domain	The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB 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 EIIA type-4 domain. Contains 1 PTS EIIB type-4 domain.

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Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cell inner membrane Cell membrane Cytoplasm Membrane
Molecular function	Kinase Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing
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 integral to membrane Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct 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...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
cytR	P0ACN7	1	EBI-554089,EBI-1125696

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6

Chain

2 – 323

322

PTS system mannose-specific EIIAB component

PRO_0000186653

Regions

Domain

2 – 124

123

PTS EIIA type-4

Domain

157 – 320

164

PTS EIIB type-4

Region

137 – 155

Hinge

Sites

Active site

Tele-phosphohistidine intermediate; for EIIA activity By similarity

Active site

175

Pros-phosphohistidine intermediate; for EIIB activity By similarity

Amino acid modifications

Modified residue

N6-acetyllysine Ref.8

Modified residue

234

N6-acetyllysine Ref.8

Experimental info

Sequence conflict

2 – 23

TIAIV…KTAEM → GWGCRAGCLKRQKW in AAA24110. Ref.1

Sequence conflict

D → N in AAA24110. Ref.1

Sequence conflict

101

T → R in AAA24110. Ref.1

Sequence conflict

142

A → G in AAA24110. Ref.1

Secondary structure

323

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P69797-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A446B79421B8C040
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FASTA

323

35,048

        10         20         30         40         50         60 
MTIAIVIGTH GWAAEQLLKT AEMLLGEQEN VGWIDFVPGE NAETLIEKYN AQLAKLDTTK 

        70         80         90        100        110        120 
GVLFLVDTWG GSPFNAASRI VVDKEHYEVI AGVNIPMLVE TLMARDDDPS FDELVALAVE 

       130        140        150        160        170        180 
TGREGVKALK AKPVEKAAPA PAAAAPKAAP TPAKPMGPND YMVIGLARID DRLIHGQVAT 

       190        200        210        220        230        240 
RWTKETNVSR IIVVSDEVAA DTVRKTLLTQ VAPPGVTAHV VDVAKMIRVY NNPKYAGERV 

       250        260        270        280        290        300 
MLLFTNPTDV ERLVEGGVKI TSVNVGGMAF RQGKTQVNNA VSVDEKDIEA FKKLNARGIE 

       310        320 
LEVRKVSTDP KLKMMDLISK IDK

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of manX(ptsL) encoding the enzyme III(Man) (II-A(Man)) function in the phosphotransferase system of Escherichia coli K-12." Saris P.E.J., Liljestroem P., Palva E.T. FEMS Microbiol. Lett. 49:69-73(1988) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"The mannose permease of Escherichia coli consists of three different proteins. Amino acid sequence and function in sugar transport, sugar phosphorylation, and penetration of phage lambda DNA." Erni B., Zanolari B., Kocher H.P. J. Biol. Chem. 262:5238-5247(1987) [PubMed: 2951378] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. Horiuchi T. DNA Res. 3:379-392(1996) [PubMed: 9097040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"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.
[5]	"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.
[6]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[7]	"Protein complexes of the Escherichia coli cell envelope." Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O. J. Biol. Chem. 280:34409-34419(2005) [PubMed: 16079137] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: BL21-DE3.
[8]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55 AND LYS-234, MASS SPECTROMETRY.
[9]	"Structure of the IIA domain of the mannose transporter from Escherichia coli at 1.7-A resolution." Nunn R.S., Markovic-Housley Z., Genovesio-Taverne J.-C., Fluekiger K., Rizkallah P.J., Jansonius J.N., Schirmer T., Erni B. J. Mol. Biol. 259:502-511(1996) [PubMed: 8676384] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-134.
[10]	"Predicted topology of the N-terminal domain of the hydrophilic subunit of the mannose transporter of Escherichia coli." Markovic-Housley Z., Balbach J., Stolz B., Genovesio-Taverne J.-C. FEBS Lett. 340:202-206(1994) [PubMed: 8131846] [Abstract] Cited for: STRUCTURE BY NMR OF 1-121.
[11]	"Secondary structure of the IIB domain of the Escherichia coli mannose transporter, a new fold in the class of alpha/beta twisted open-sheet structures." Gschwind R.M., Gemmecker G., Leutner M., Kessler H., Gutknecht R., Lanz R., Fluekiger K., Erni B. FEBS Lett. 404:45-50(1997) [PubMed: 9074635] [Abstract] Cited for: STRUCTURE BY NMR OF 156-323.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

M36404 Genomic DNA. Translation: AAA24110.1.
J02699 Genomic DNA. Translation: AAA24443.1.
U00096 Genomic DNA. Translation: AAC74887.1.
AP009048 Genomic DNA. Translation: BAA15624.1.

PIR

WQECM3. A30286.

RefSeq

AP_002436.1.
NP_416331.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PDO	X-ray	1.70	A	2-133	[»]
1VRC	NMR	-	A/B	2-132	[»]
1VSQ	NMR	-	A/B	2-134	[»]
			C	159-323	[»]
2JZH	NMR	-	A	154-323	[»]
2JZN	NMR	-	A/B	2-134	[»]
			C	159-323	[»]
2JZO	NMR	-	A/B	2-134	[»]
			D	159-323	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P69797. 12 interactions.

Protein family/group databases

TCDB

4.A.6.1.1. PTS mannose-fructose-sorbose (Man) family.

PTM databases

PhosSite

P69797.

2-D gel databases

SWISS-2DPAGE

P69797.

Genome annotation databases

GeneID

946334.

GenomeReviews

Gene locus JW1806 in contig AP009048_GR.
Gene locus b1817 in contig U00096_GR.

KEGG

ecj:JW1806.
eco:b1817.

Organism-specific databases

EchoBASE

EB0562.

EcoGene

EG10567. manX.

CMR

Search...

Phylogenomic databases

HOGENOM

P69797.

OMA

P69797. PSEGPDD.

Enzyme and pathway databases

BioCyc

EcoCyc:MANX-MON.

Family and domain databases

InterPro

IPR004701. PTS_EIIA_fruc.
IPR013789. PTS_EIIA_fruc_sub.
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

PF03610. EIIA-man. 1 hit.
PF03830. PTSIIB_sorb. 1 hit.
[Graphical view]

ProDom

PD008332. PTSIIB_sorb. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00824. EIIA-man. 1 hit.
TIGR00854. pts-sorbose. 1 hit.

PROSITE

PS51096. PTS_EIIA_TYPE_4. 1 hit.
PS51101. PTS_EIIB_TYPE_4. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

PTNAB_ECOLI

Accession

Primary (citable) accession number: P69797
Secondary accession number(s): P08186, Q47350

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents