Reviewed, UniProtKB/Swiss-Prot O69250 (PTHP_BACME)

Names and origin

Protein names

Recommended name:
Phosphocarrier protein HPr
EC=2.7.11.-

Alternative name(s):
Histidine-containing protein

Gene names

Name:

ptsH

Organism

Bacillus megaterium

Taxonomic identifier

1404 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	88 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the permease (enzymes II/III) By similarity. P-Ser-HPr interacts with the catabolite control protein A (ccpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity By similarity.
Catalytic activity	Protein HPr N(pi)-phospho-L-histidine + protein EIIA = protein HPr + protein EIIA N(tau)-phospho-L-histidine.
Enzyme regulation	Phosphorylation on Ser-46 inhibits the phosphoryl transfer from enzyme I to HPr By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the HPr family. Contains 1 HPr domain.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transcription Transcription regulation Transport
Cellular component	Cytoplasm
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cellular transcription Inferred from electronic annotation. Source: UniProtKB-KW phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW regulation of cellular transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	kinase activity Inferred from electronic annotation. Source: UniProtKB-KW 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 – 88

88

Phosphocarrier protein HPr

PRO_0000107839

Regions

Domain

1 – 88

88

HPr

Sites

Active site

15

1

Pros-phosphohistidine intermediate By similarity

Amino acid modifications

Modified residue

12

1

Phosphoserine By similarity

Modified residue

46

1

Phosphoserine; by HPrK/P Ref.2 Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

88

Helix Strand Turn

Details...

Beta strand

3 – 7

5

Helix

16 – 25

10

Beta strand

28 – 37

10

Beta strand

40 – 43

4

Helix

47 – 50

4

Turn

51 – 53

3

Beta strand

60 – 67

8

Helix

70 – 74

5

Helix

76 – 83

8

Sequences

	Sequence		Length	Mass (Da)
	O69250-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 4EDC85C2E0B9AA3B	FASTA	88	9,119
	10 20 30 40 50 60 MAQKTFTVTA DSGIHARPAT TLVQAASKFD SDINLEFNGK TVNLKSIMGV MSLGIQKGAT 70 80 ITISAEGSDE ADALAALEDT MSKEGLGE

References

[1]	"Sequence of ptsH and ptsI of Bacillus megaterium." Wagner A., Kuester E., Hillen W. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: WH348.
[2]	"Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P." Schumacher M.A., Allen G.S., Diel M., Seidel G., Hillen W., Brennan R.G. Cell 118:731-741(2004) [PubMed: 15369672] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), PHOSPHORYLATION AT SER-46.
[3]	"Structural mechanism for the fine-tuning of CcpA function by the small molecule effectors glucose 6-phosphate and fructose 1,6-bisphosphate." Schumacher M.A., Seidel G., Hillen W., Brennan R.G. J. Mol. Biol. 368:1042-1050(2007) [PubMed: 17376479] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), PHOSPHORYLATION AT SER-46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ005075 Genomic DNA. Translation: CAA06331.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RZR	X-ray	2.80	L/S/T/Y	1-88	[»]
2NZU	X-ray	2.50	L	1-88	[»]
2NZV	X-ray	3.00	L	1-88	[»]
2OEN	X-ray	3.17	L	1-88	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR001020. PTS_HPr_His_P_site.
IPR005698. PTS_HPr_prot.
IPR000032. PTS_HPr_prot-like.
IPR002114. PTS_HPr_Ser_P_site.
[Graphical view]

Gene3D

G3DSA:3.30.1340.10. PTS_HPr_protein. 1 hit.

Pfam

PF00381. PTS-HPr. 1 hit.
[Graphical view]

PRINTS

PR00107. PHOSPHOCPHPR.

SUPFAM

SSF55594. HPr_protein. 1 hit.

TIGRFAMs

TIGR01003. PTS_HPr_family. 1 hit.

PROSITE

PS51350. PTS_HPR_DOM. 1 hit.
PS00369. PTS_HPR_HIS. 1 hit.
PS00589. PTS_HPR_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PTHP_BACME

Accession

Primary (citable) accession number: O69250

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	August 1, 1998
Last modified:	March 2, 2010
This is version 64 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)