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Protein

PTS system mannitol-specific EIICBA component

Gene

mtlA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

[Protein]-N(pi)-phospho-L-histidine + D-mannitol(Side 1) = [protein]-L-histidine + D-mannitol 1-phosphate(Side 2).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei384 – 3841Phosphocysteine intermediate; for EIIB activity
Active sitei554 – 5541Tele-phosphohistidine intermediate; for EIIA activity

GO - Molecular functioni

GO - Biological processi

  • carbohydrate transmembrane transport Source: GOC
  • mannitol transport Source: EcoCyc
  • phosphoenolpyruvate-dependent sugar phosphotransferase system Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Phosphotransferase system, Sugar transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:MTLA-MONOMER.
ECOL316407:JW3573-MONOMER.
MetaCyc:MTLA-MONOMER.

Protein family/group databases

TCDBi4.A.2.1.2. the pts fructose-mannitol (fru) family.

Names & Taxonomyi

Protein namesi
Recommended name:
PTS system mannitol-specific EIICBA component
Alternative name(s):
EIICBA-Mtl
Short name:
EII-Mtl
Including the following 3 domains:
Mannitol permease IIC component
Alternative name(s):
PTS system mannitol-specific EIIC component
Mannitol-specific phosphotransferase enzyme IIB component (EC:2.7.1.197)
Alternative name(s):
PTS system mannitol-specific EIIB component
Mannitol-specific phosphotransferase enzyme IIA component
Alternative name(s):
PTS system mannitol-specific EIIA component
Gene namesi
Name:mtlA
Ordered Locus Names:b3599, JW3573
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10615. mtlA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2424CytoplasmicSequence analysisAdd
BLAST
Transmembranei25 – 4420HelicalCuratedAdd
BLAST
Topological domaini45 – 506PeriplasmicSequence analysis
Transmembranei51 – 6919HelicalCuratedAdd
BLAST
Topological domaini70 – 13465CytoplasmicSequence analysisAdd
BLAST
Transmembranei135 – 15420HelicalCuratedAdd
BLAST
Topological domaini155 – 16511PeriplasmicSequence analysisAdd
BLAST
Transmembranei166 – 18419HelicalCuratedAdd
BLAST
Topological domaini185 – 27389CytoplasmicSequence analysisAdd
BLAST
Transmembranei274 – 29118HelicalCuratedAdd
BLAST
Topological domaini292 – 31322PeriplasmicSequence analysisAdd
BLAST
Transmembranei314 – 33320HelicalCuratedAdd
BLAST
Topological domaini334 – 637304Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 637637PTS system mannitol-specific EIICBA componentPRO_0000186614Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei384 – 3841Phosphocysteine1 Publication
Modified residuei554 – 5541Phosphohistidine1 Publication

Post-translational modificationi

An intramolecular phosphotransfer takes places between His-554 and Cys-384.

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP00550.
PaxDbiP00550.
PRIDEiP00550.

PTM databases

iPTMnetiP00550.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4260741. 9 interactions.
DIPiDIP-10267N.
IntActiP00550. 2 interactions.
MINTiMINT-245984.
STRINGi511145.b3599.

Structurei

Secondary structure

1
637
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi379 – 3824Combined sources
Beta strandi385 – 3884Combined sources
Helixi389 – 40416Combined sources
Beta strandi410 – 4145Combined sources
Beta strandi425 – 4306Combined sources
Helixi431 – 44010Combined sources
Beta strandi444 – 4507Combined sources
Helixi455 – 47016Combined sources
Helixi498 – 5003Combined sources
Helixi510 – 52314Combined sources
Helixi530 – 54112Combined sources
Beta strandi545 – 5473Combined sources
Helixi557 – 5626Combined sources
Beta strandi563 – 5653Combined sources
Beta strandi567 – 57812Combined sources
Beta strandi580 – 5823Combined sources
Beta strandi586 – 5949Combined sources
Turni597 – 5993Combined sources
Helixi600 – 61011Combined sources
Helixi614 – 6229Combined sources
Helixi626 – 6327Combined sources
Turni633 – 6353Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A3AX-ray1.80A/B/C/D491-637[»]
1J6TNMR-A491-637[»]
1VKRNMR-A367-489[»]
1VRVNMR-A375-475[»]
2FEWNMR-A491-637[»]
B375-475[»]
ProteinModelPortaliP00550.
SMRiP00550. Positions 375-471, 492-637.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00550.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 341330PTS EIIC type-2PROSITE-ProRule annotationAdd
BLAST
Domaini378 – 47396PTS EIIB type-2PROSITE-ProRule annotationAdd
BLAST
Domaini494 – 636143PTS EIIA type-2PROSITE-ProRule annotationAdd
BLAST

Domaini

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.

Sequence similaritiesi

Contains 1 PTS EIIA type-2 domain.PROSITE-ProRule annotation
Contains 1 PTS EIIB type-2 domain.PROSITE-ProRule annotation
Contains 1 PTS EIIC type-2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CTS. Bacteria.
COG2213. LUCA.
COG4668. LUCA.
HOGENOMiHOG000252814.
InParanoidiP00550.
KOiK02798.
K02799.
K02800.
OMAiGWAIKRF.
OrthoDBiEOG6FBWWQ.
PhylomeDBiP00550.

Family and domain databases

Gene3Di3.40.50.10370. 1 hit.
3.40.930.10. 1 hit.
InterProiIPR016152. PTrfase/Anion_transptr.
IPR002178. PTS_EIIA_type-2_dom.
IPR013011. PTS_EIIB_2.
IPR003501. PTS_EIIB_2/3.
IPR029503. PTS_EIIB_mannitol.
IPR003352. PTS_EIIC.
IPR013014. PTS_EIIC_2.
IPR004718. PTS_IIC_mtl.
[Graphical view]
PfamiPF00359. PTS_EIIA_2. 1 hit.
PF02378. PTS_EIIC. 1 hit.
PF02302. PTS_IIB. 1 hit.
[Graphical view]
SUPFAMiSSF52794. SSF52794. 1 hit.
SSF55804. SSF55804. 1 hit.
TIGRFAMsiTIGR00851. mtlA. 1 hit.
PROSITEiPS51094. 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]

Sequencei

Sequence statusi: Complete.

P00550-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSDIKIKVQ SFGRFLSNMV MPNIGAFIAW GIITALFIPT GWLPNETLAK
60 70 80 90 100
LVGPMITYLL PLLIGYTGGK LVGGERGGVV GAITTMGVIV GADMPMFLGS
110 120 130 140 150
MIAGPLGGWC IKHFDRWVDG KIKSGFEMLV NNFSAGIIGM ILAILAFLGI
160 170 180 190 200
GPIVEALSKM LAAGVNFMVV HDMLPLASIF VEPAKILFLN NAINHGIFSP
210 220 230 240 250
LGIQQSHELG KSIFFLIEAN PGPGMGVLLA YMFFGRGSAK QSAGGAAIIH
260 270 280 290 300
FLGGIHEIYF PYVLMNPRLI LAVILGGMTG VFTLTILGGG LVSPASPGSI
310 320 330 340 350
LAVLAMTPKG AYFANIAGVC AAMAVSFVVS AILLKTSKVK EEDDIEAATR
360 370 380 390 400
RMQDMKAESK GASPLSAGDV TNDLSHVRKI IVACDAGMGS SAMGAGVLRK
410 420 430 440 450
KIQDAGLSQI SVTNSAINNL PPDVDLVITH RDLTERAMRQ VPQAQHISLT
460 470 480 490 500
NFLDSGLYTS LTERLVAAQR HTANEEKVKD SLKDSFDDSS ANLFKLGAEN
510 520 530 540 550
IFLGRKAATK EEAIRFAGEQ LVKGGYVEPE YVQAMLDREK LTPTYLGESI
560 570 580 590 600
AVPHGTVEAK DRVLKTGVVF CQYPEGVRFG EEEDDIARLV IGIAARNNEH
610 620 630
IQVITSLTNA LDDESVIERL AHTTSVDEVL ELLAGRK
Length:637
Mass (Da):67,972
Last modified:July 21, 1986 - v1
Checksum:iA992992D534BF98D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA00661. WQEC2M.
RefSeqiNP_418056.1. NC_000913.3.
WP_000093247.1. NZ_CP014272.1.

Genome annotation databases

EnsemblBacteriaiAAC76623; AAC76623; b3599.
BAE77694; BAE77694; BAE77694.
GeneIDi948118.
KEGGiecj:JW3573.
eco:b3599.
PATRICi32122681. VBIEscCol129921_3717.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA00661. WQEC2M.
RefSeqiNP_418056.1. NC_000913.3.
WP_000093247.1. NZ_CP014272.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A3AX-ray1.80A/B/C/D491-637[»]
1J6TNMR-A491-637[»]
1VKRNMR-A367-489[»]
1VRVNMR-A375-475[»]
2FEWNMR-A491-637[»]
B375-475[»]
ProteinModelPortaliP00550.
SMRiP00550. Positions 375-471, 492-637.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260741. 9 interactions.
DIPiDIP-10267N.
IntActiP00550. 2 interactions.
MINTiMINT-245984.
STRINGi511145.b3599.

Protein family/group databases

TCDBi4.A.2.1.2. the pts fructose-mannitol (fru) family.

PTM databases

iPTMnetiP00550.

Proteomic databases

EPDiP00550.
PaxDbiP00550.
PRIDEiP00550.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76623; AAC76623; b3599.
BAE77694; BAE77694; BAE77694.
GeneIDi948118.
KEGGiecj:JW3573.
eco:b3599.
PATRICi32122681. VBIEscCol129921_3717.

Organism-specific databases

EchoBASEiEB0610.
EcoGeneiEG10615. mtlA.

Phylogenomic databases

eggNOGiENOG4105CTS. Bacteria.
COG2213. LUCA.
COG4668. LUCA.
HOGENOMiHOG000252814.
InParanoidiP00550.
KOiK02798.
K02799.
K02800.
OMAiGWAIKRF.
OrthoDBiEOG6FBWWQ.
PhylomeDBiP00550.

Enzyme and pathway databases

BioCyciEcoCyc:MTLA-MONOMER.
ECOL316407:JW3573-MONOMER.
MetaCyc:MTLA-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP00550.
PROiP00550.

Family and domain databases

Gene3Di3.40.50.10370. 1 hit.
3.40.930.10. 1 hit.
InterProiIPR016152. PTrfase/Anion_transptr.
IPR002178. PTS_EIIA_type-2_dom.
IPR013011. PTS_EIIB_2.
IPR003501. PTS_EIIB_2/3.
IPR029503. PTS_EIIB_mannitol.
IPR003352. PTS_EIIC.
IPR013014. PTS_EIIC_2.
IPR004718. PTS_IIC_mtl.
[Graphical view]
PfamiPF00359. PTS_EIIA_2. 1 hit.
PF02378. PTS_EIIC. 1 hit.
PF02302. PTS_IIB. 1 hit.
[Graphical view]
SUPFAMiSSF52794. SSF52794. 1 hit.
SSF55804. SSF55804. 1 hit.
TIGRFAMsiTIGR00851. mtlA. 1 hit.
PROSITEiPS51094. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT CYS-384 AND 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 490-637.

Entry informationi

Entry nameiPTM3C_ECOLI
AccessioniPrimary (citable) accession number: P00550
Secondary accession number(s): Q2M7R2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 11, 2016
This is version 173 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.