P0A0E3 (PTHP_STAAU) Reviewed, UniProtKB/Swiss-Prot

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

Staphylococcus aureus

Taxonomic identifier

1280 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus

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). 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.
Subcellular location	Cytoplasm.
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 Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	protein serine/threonine 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_0000107878

Regions

Domain

1 – 88

88

HPr

Sites

Active site

15

1

Pros-phosphohistidine intermediate

Amino acid modifications

Modified residue

46

1

Phosphoserine; by HPrK/P

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

88

Helix Strand Turn

Details...

Beta strand

2 – 8

7

Helix

16 – 29

14

Beta strand

30 – 37

8

Beta strand

40 – 43

4

Helix

47 – 51

5

Turn

52 – 54

3

Beta strand

60 – 69

10

Helix

70 – 84

15

Sequences

	Sequence		Length	Mass (Da)
	P0A0E3 [UniParc]. Last modified March 1, 2005. Version 1. Checksum: B2C6639D53226FF9	FASTA	88	9,496
	10 20 30 40 50 60 MEQNSYVIID ETGIHARPAT MLVQTASKFD SDIQLEYNGK KVNLKSIMGV MSLGVGKDAE 70 80 ITIYADGSDE SDAIQAISDV LSKEGLTK

References

[1]	Kravanja M., Engelmann R., Christiansen I., Hengstenberg W. Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 305A.
[2]	"The phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus aureus. 1. Amino-acid sequence of the phosphocarrier protein HPr." Beyreuther K., Raufuss H., Schrecker O., Hengstenberg W. Eur. J. Biochem. 75:275-286(1977) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE.
[3]	"The phosphoenolpyruvate:sugar phosphotransferase system in Gram-positive bacteria: properties, mechanism, and regulation." Reizer J., Saier M.H. Jr., Deutscher J., Grenier F., Thompson J., Hengstenberg W. Crit. Rev. Microbiol. 15:297-338(1988) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[4]	"Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure." Kalbitzer H.R., Neidig K.-P., Hengstenberg W. Biochemistry 30:11186-11192(1991) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[5]	"The solution structure of the histidine-containing protein (HPr) from Staphylococcus aureus as determined by two-dimensional 1H-NMR spectroscopy." Kalbitzer H.R., Hengstenberg W. Eur. J. Biochem. 216:205-214(1993) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X93205 Genomic DNA. Translation: CAA63688.1.

PIR

WPSAHP. A03404.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KA5	NMR	-	A	1-88	[»]

ProteinModelPortal

P0A0E3.

SMR

P0A0E3. Positions 1-88.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

eggNOG

COG1925.

Family and domain databases

Gene3D

3.30.1340.10. 1 hit.

InterPro

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

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...

Other

EvolutionaryTrace

P0A0E3.

Entry information

Entry name

PTHP_STAAU

Accession

Primary (citable) accession number: P0A0E3
Secondary accession number(s): P02907

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	March 1, 2005
Last modified:	April 3, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program