Reviewed, UniProtKB/Swiss-Prot P75061 (PTHP_MYCPN)

Names and origin

Protein names

Recommended name:
    Phosphocarrier protein HPr
    EC=2.7.11.-
Alternative name(s):
    Histidine-containing protein

Gene names

Name:	ptsH
Ordered Locus Names:	MPN_053
ORF Names:	MP101

Organism

Mycoplasma pneumoniae [Complete proteome] [HAMAP]

Taxonomic identifier

2104 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma

Protein attributes

Sequence length	88 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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-47 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	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW 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_0000107864
Regions
	Domain	1 – 88	88	HPr
Sites
	Active site	15	1	Pros-phosphohistidine intermediate By similarity
Amino acid modifications
	Modified residue	47	1	Phosphoserine; by HPrK/P Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P75061-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 5609A9F8F9E2C1FE	FASTA	88	9,495
	10 20 30 40 50 60 MKKIQVVVKD PVGIHARPAS IIAGEANKFK SELKLVSPSG VEGNIKSIIN LMSLGIKQND 70 80 HITIKAEGTD EEEALNAIKA VLEKHQVI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae." Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R. Nucleic Acids Res. 24:4420-4449(1996) [PubMed: 8948633] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29342 / M129.
[2]	"Towards a two-dimensional proteome map of Mycoplasma pneumoniae." Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., Herrmann R., Frank R. Electrophoresis 21:3765-3780(2000) [PubMed: 11271496] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY. Strain: ATCC 29342 / M129.
[3]	"A novel mode of control of Mycoplasma pneumoniae HPr kinase/phosphatase activity reflects its parasitic lifestyle." Steinhauer K., Jepp T., Hillen W., Stuelke J. Microbiology 148:3277-3284(2002) [PubMed: 12368461] [Abstract] Cited for: PHOSPHORYLATION.
[4]	"Proteogenomic mapping as a complementary method to perform genome annotation." Jaffe J.D., Berg H.C., Church G.M. Proteomics 4:59-77(2004) [PubMed: 14730672] [Abstract] Cited for: PHOSPHORYLATION AT SER-47, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U00089 Genomic DNA. Translation: AAB95749.1.
PIR	S73427.
RefSeq	NP_109741.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	876864.
GenomeReviews	Gene locus MPN_053 in contig U00089_GR.
KEGG	mpn:MPN053.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P75061.
OMA	PVGIHAR
Enzyme and pathway databases
BioCyc	MPNE272634:MPN053-MON.
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.
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_MYCPN

Accession

Primary (citable) accession number: P75061

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	November 24, 2009
This is version 68 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)