Reviewed, UniProtKB/Swiss-Prot P69798 (PTNAB_ECOL6)

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
Ordered Locus Names:	c2223

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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 By similarity.
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 By similarity.
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.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cytoplasm
Molecular function	Kinase Transferase
PTM	Acetylation
Technical term	Complete proteome
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
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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 323	322	PTS system mannose-specific EIIAB component		PRO_0000186654
Regions
	Domain	2 – 124	123	PTS EIIA type-4
	Domain	157 – 320	164	PTS EIIB type-4
	Region	137 – 155	19	Hinge
Sites
	Active site	10	1	Tele-phosphohistidine intermediate; for EIIA activity By similarity
	Active site	175	1	Pros-phosphohistidine intermediate; for EIIB activity By similarity
Amino acid modifications
	Modified residue	55	1	N6-acetyllysine By similarity
	Modified residue	234	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P69798-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: A446B79421B8C040	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

References

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014075 Genomic DNA. Translation: AAN80682.1.
RefSeq	NP_754117.1.
3D structure databases
SMR	P69798. Positions 2-130.
ModBase	Search...
Genome annotation databases
GeneID	1036702.
GenomeReviews	Gene locus c2223 in contig AE014075_GR.
KEGG	ecc:c2223.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P69798.
OMA	P69798. PSEGPDD.
Enzyme and pathway databases
BRENDA	2.7.1.69. 292881.
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...

Entry information

Entry name

PTNAB_ECOL6

Accession

Primary (citable) accession number: P69798
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 35 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)