PTS system mannitol-specific EIICBA component - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P00550 (PTM3C_ECOLI)

Last modified June 16, 2009. Version 113. 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 mannitol-specific EIICBA component
Alternative name(s):
    EIICBA-Mtl
      Short name=EII-Mtl
Including the following 3 domains:
    1- Recommended name:
            Mannitol permease IIC component
        Alternative name(s):
            PTS system mannitol-specific EIIC component
    2- Recommended name:
            Mannitol-specific phosphotransferase enzyme IIB component
              EC=2.7.1.69
        Alternative name(s):
            PTS system mannitol-specific EIIB component
    3- Recommended name:
            Mannitol-specific phosphotransferase enzyme IIA component
              EC=2.7.1.-
        Alternative name(s):
            PTS system mannitol-specific EIIA component

Gene names

Name:	mtlA
Ordered Locus Names:	b3599, JW3573

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	637 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 mannitol 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.
Subunit structure	Homodimer.
Subcellular location	Cell inner membrane; Multi-pass membrane protein. Ref.8
Domain	The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site. 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 EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.
Post-translational modification	An intramolecular phosphotransfer takes places between His-554 and Cys-384.
Sequence similarities	Contains 1 PTS EIIA type-2 domain. Contains 1 PTS EIIB type-2 domain. Contains 1 PTS EIIC type-2 domain.

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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	3D-structure 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 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
groL	P0A6F5	1	EBI-547239,EBI-543750

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 637

637

PTS system mannitol-specific EIICBA component

PRO_0000186614

Regions

Topological domain

1 – 24

Cytoplasmic Potential

Transmembrane

25 – 44

Probable

Topological domain

45 – 50

Periplasmic Potential

Transmembrane

51 – 69

Probable

Topological domain

70 – 134

Cytoplasmic Potential

Transmembrane

135 – 154

Probable

Topological domain

155 – 165

Periplasmic Potential

Transmembrane

166 – 184

Probable

Topological domain

185 – 273

Cytoplasmic Potential

Transmembrane

274 – 291

Probable

Topological domain

292 – 313

Periplasmic Potential

Transmembrane

314 – 333

Probable

Topological domain

334 – 637

304

Cytoplasmic Probable

Domain

12 – 341

330

PTS EIIC type-2

Domain

378 – 473

PTS EIIB type-2

Domain

494 – 636

143

PTS EIIA type-2

Sites

Active site

384

Phosphocysteine intermediate; for EIIB activity Ref.6

Active site

554

Tele-phosphohistidine intermediate; for EIIA activity Ref.6

Secondary structure

637

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P00550-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: A992992D534BF98D
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FASTA

637

67,972

        10         20         30         40         50         60 
MSSDIKIKVQ SFGRFLSNMV MPNIGAFIAW GIITALFIPT GWLPNETLAK LVGPMITYLL 

        70         80         90        100        110        120 
PLLIGYTGGK LVGGERGGVV GAITTMGVIV GADMPMFLGS MIAGPLGGWC IKHFDRWVDG 

       130        140        150        160        170        180 
KIKSGFEMLV NNFSAGIIGM ILAILAFLGI GPIVEALSKM LAAGVNFMVV HDMLPLASIF 

       190        200        210        220        230        240 
VEPAKILFLN NAINHGIFSP LGIQQSHELG KSIFFLIEAN PGPGMGVLLA YMFFGRGSAK 

       250        260        270        280        290        300 
QSAGGAAIIH FLGGIHEIYF PYVLMNPRLI LAVILGGMTG VFTLTILGGG LVSPASPGSI 

       310        320        330        340        350        360 
LAVLAMTPKG AYFANIAGVC AAMAVSFVVS AILLKTSKVK EEDDIEAATR RMQDMKAESK 

       370        380        390        400        410        420 
GASPLSAGDV TNDLSHVRKI IVACDAGMGS SAMGAGVLRK KIQDAGLSQI SVTNSAINNL 

       430        440        450        460        470        480 
PPDVDLVITH RDLTERAMRQ VPQAQHISLT NFLDSGLYTS LTERLVAAQR HTANEEKVKD 

       490        500        510        520        530        540 
SLKDSFDDSS ANLFKLGAEN IFLGRKAATK EEAIRFAGEQ LVKGGYVEPE YVQAMLDREK 

       550        560        570        580        590        600 
LTPTYLGESI AVPHGTVEAK DRVLKTGVVF CQYPEGVRFG EEEDDIARLV IGIAARNNEH 

       610        620        630 
IQVITSLTNA LDDESVIERL AHTTSVDEVL ELLAGRK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mannitol-specific enzyme II of the bacterial phosphotransferase system. III. The nucleotide sequence of the permease gene." Lee C.A., Saier M.H. Jr. J. Biol. Chem. 258:10761-10767(1983) [PubMed: 6309813] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R. Nucleic Acids Res. 22:2576-2586(1994) [PubMed: 8041620] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"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.
[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]	"Nucleotide sequence of the mannitol (mtl) operon in Escherichia coli." Davis T., Yamada M., Elgort M., Saier M.H. Jr. Mol. Microbiol. 2:405-412(1988) [PubMed: 3135464] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 619-637. Strain: K12.
[6]	"S-phosphocysteine and phosphohistidine are intermediates in the phosphoenolpyruvate-dependent mannitol transport catalyzed by Escherichia coli EIIMtl." Pas H.H., Robillard G.T. Biochemistry 27:5835-5839(1988) [PubMed: 3142516] [Abstract] Cited for: PHOSPHORYLATION AT HIS-554.
[7]	"Membrane topology analysis of Escherichia coli mannitol permease by using a nested-deletion method to create mtlA-phoA fusions." Sugiyama J.E., Mahmoodian S., Jacobson G.R. Proc. Natl. Acad. Sci. U.S.A. 88:9603-9607(1991) [PubMed: 1946374] [Abstract] Cited for: TOPOLOGY.
[8]	"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.
[9]	"The structure of the Escherichia coli phosphotransferase IIAmannitol reveals a novel fold with two conformations of the active site." van Montfort R.L.M., Pijning T., Kalk K.H., Hangyi I., Kouwijzer M.L.C.E., Robillard G.T., Dijkstra B.W. Structure 6:377-388(1998) [PubMed: 9551558] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 490-637.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

V01503 Genomic DNA. Translation: CAA24748.1.
U00039 Genomic DNA. Translation: AAB18576.1.
U00096 Genomic DNA. Translation: AAC76623.1.
AP009048 Genomic DNA. Translation: BAE77694.1.
X06794 Genomic DNA. Translation: CAA29953.1.

PIR

WQEC2M. A00661.

RefSeq

AP_004193.1.
NP_418056.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A3A	X-ray	1.80	A/B/C/D	491-637	[»]
1J6T	NMR	-	A	491-637	[»]
1VKR	NMR	-	A	367-489	[»]
1VRV	NMR	-	A	375-475	[»]
2FEW	NMR	-	A	491-637	[»]
			B	375-475	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:10267N.

IntAct

P00550. 2 interactions.

Protein family/group databases

TCDB

4.A.2.1.2. PTS fructose-mannitol (Fru) family.

Genome annotation databases

GeneID

948118.

GenomeReviews

Gene locus JW3573 in contig AP009048_GR.
Gene locus b3599 in contig U00096_GR.

KEGG

ecj:JW3573.
eco:b3599.

Organism-specific databases

EchoBASE

EB0610.

EcoGene

EG10615. mtlA.

CMR

Search...

Phylogenomic databases

HOGENOM

P00550.

OMA

P00550. ITHKDLT.

Enzyme and pathway databases

BioCyc

EcoCyc:MTLA-MON.

Family and domain databases

InterPro

IPR002178. PTS_EIIA_2.
IPR013011. PTS_EIIB_2.
IPR003352. PTS_EIIC.
IPR013014. PTS_EIIC_2.
IPR003501. PTS_IIB_lac.
IPR004718. PTS_IIC_mtl.
[Graphical view]

Gene3D

G3DSA:3.40.930.10. PTS_EIIA_2. 1 hit.

Pfam

PF00359. PTS_EIIA_2. 1 hit.
PF02378. PTS_EIIC. 1 hit.
PF02302. PTS_IIB. 1 hit.
[Graphical view]

ProDom

PD001689. PTS_EIIA_2. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00851. mtlA. 1 hit.

PROSITE

PS51094. PTS_EIIA_TYPE_2. 1 hit.
PS00372. PTS_EIIA_TYPE_2_HIS. 1 hit.
PS51099. PTS_EIIB_TYPE_2. 1 hit.
PS51104. PTS_EIIC_TYPE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

PTM3C_ECOLI

Accession

Primary (citable) accession number: P00550
Secondary accession number(s): Q2M7R2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 113 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)

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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

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents