P00550 (PTM3C_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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. Mannitol permease IIC component
   Alternative name(s):
   PTS system mannitol-specific EIIC component
2. Mannitol-specific phosphotransferase enzyme IIB component
   EC=2.7.1.69
   Alternative name(s):
   PTS system mannitol-specific EIIB component
3. 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)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	637 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Reference 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: InterPro
Complete GO annotation...

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

24

Cytoplasmic Potential

Transmembrane

25 – 44

20

Helical; Probable

Topological domain

45 – 50

6

Periplasmic Potential

Transmembrane

51 – 69

19

Helical; Probable

Topological domain

70 – 134

65

Cytoplasmic Potential

Transmembrane

135 – 154

20

Helical; Probable

Topological domain

155 – 165

11

Periplasmic Potential

Transmembrane

166 – 184

19

Helical; Probable

Topological domain

185 – 273

89

Cytoplasmic Potential

Transmembrane

274 – 291

18

Helical; Probable

Topological domain

292 – 313

22

Periplasmic Potential

Transmembrane

314 – 333

20

Helical; Probable

Topological domain

334 – 637

304

Cytoplasmic Probable

Domain

12 – 341

330

PTS EIIC type-2

Domain

378 – 473

96

PTS EIIB type-2

Domain

494 – 636

143

PTS EIIA type-2

Sites

Active site

384

1

Phosphocysteine intermediate; for EIIB activity Ref.6

Active site

554

1

Tele-phosphohistidine intermediate; for EIIA activity Ref.6

Secondary structure

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637

Helix Strand Turn

Details...

Beta strand

379 – 389

11

Helix

390 – 404

15

Beta strand

410 – 416

7

Beta strand

425 – 430

6

Helix

431 – 440

10

Beta strand

444 – 450

7

Helix

455 – 470

16

Helix

498 – 500

3

Helix

510 – 523

14

Helix

530 – 541

12

Beta strand

545 – 547

3

Helix

557 – 562

6

Beta strand

563 – 565

3

Beta strand

567 – 578

12

Beta strand

580 – 582

3

Beta strand

586 – 594

9

Turn

597 – 599

3

Helix

600 – 610

11

Helix

614 – 622

9

Helix

626 – 632

7

Turn

633 – 635

3

Sequences

	Sequence		Length	Mass (Da)
	P00550 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: A992992D534BF98D	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

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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

NP_418056.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P00550.

SMR

P00550. Positions 375-471, 492-637.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10267N.

IntAct

P00550. 2 interactions.

MINT

MINT-245984.

Protein family/group databases

TCDB

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

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000300; EBESCP00000000300; EBESCG00000000243.
EBESCT00000015432; EBESCP00000014723; EBESCG00000014492.

GeneID

948118.

GenomeReviews

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

KEGG

ecj:JW3573.
eco:b3599.

PATRIC

32122681. VBIEscCol129921_3717.

Organism-specific databases

EchoBASE

EB0610.

EcoGene

EG10615. mtlA.

Phylogenomic databases

eggNOG

COG2213.

GeneTree

EBGT00050000009675.

HOGENOM

HBG296680.

OMA

ITHKDLT.

PhylomeDB

P00550.

ProtClustDB

PRK15083.

Enzyme and pathway databases

BioCyc

EcoCyc:MTLA-MONOMER.

Gene expression databases

Genevestigator

P00550.

Family and domain databases

InterPro

IPR016152. PTrfase/Anion_transptr.
IPR002178. PTS_EIIA_2.
IPR013011. PTS_EIIB_2.
IPR003501. PTS_EIIB_2/3.
IPR003352. PTS_EIIC.
IPR013014. PTS_EIIC_2.
IPR004718. PTS_IIC_mtl.
[Graphical view]

Gene3D

G3DSA:3.40.930.10. PTS_EIIA_2. 1 hit.

KO

K02798.
K02799.
K02800.

Pfam

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

SUPFAM

SSF55804. PTrfase/Anion_transptr. 1 hit.

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...

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:	January 25, 2012
This is version 135 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program