P08877 (PTHP_BACSU) 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
Ordered Locus Names:	BSU13900

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	88 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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). Ref.5 Ref.6 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. Ref.5 Ref.6
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 Complete proteome Direct protein sequencing Reference proteome
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

Initiator methionine

1

1

Removed Ref.3 Ref.4

Chain

2 – 88

87

Phosphocarrier protein HPr

PRO_0000107842

Regions

Domain

2 – 88

87

HPr

Sites

Active site

15

1

Pros-phosphohistidine intermediate Ref.8 Ref.11 PubMed 7803390

Amino acid modifications

Modified residue

12

1

Phosphoserine Ref.7

Modified residue

46

1

Phosphoserine; by HPrK/P Ref.7

Experimental info

Mutagenesis

46

1

S → A: No phosphorylation by HPrK/P; abolishes the catabolite repressive effects of glucose on gluconate kinase, glucitol dehydrogenase, and the mannitol-specific catabolic enzymes. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

88

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Beta strand

10 – 12

3

Helix

16 – 26

11

Beta strand

29 – 37

9

Beta strand

40 – 43

4

Helix

47 – 53

7

Beta strand

60 – 67

8

Helix

70 – 83

14

Sequences

	Sequence		Length	Mass (Da)
	P08877 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 2B13DBD63DD636A9	FASTA	88	9,189
	10 20 30 40 50 60 MAQKTFKVTA DSGIHARPAT VLVQTASKYD ADVNLEYNGK TVNLKSIMGV MSLGIAKGAE 70 80 ITISASGADE NDALNALEET MKSEGLGE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Phosphoenolpyruvate:sugar phosphotransferase system of Bacillus subtilis: nucleotide sequence of ptsX, ptsH and the 5'-end of ptsI and evidence for a ptsHI operon." Gonzy-Treboul G., Zagorec M., Rain-Guion M.-C., Steinmetz M. Mol. Microbiol. 3:103-112(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Amino acid sequences of several Bacillus subtilis proteins modified by apparent guanylylation." Mitchell C., Morris P.W., Vary J.C. Mol. Microbiol. 6:1579-1581(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21.
[4]	"Cold shock stress-induced proteins in Bacillus subtilis." Graumann P., Schroeder K., Schmid R., Marahiel M.A. J. Bacteriol. 178:4611-4619(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-27. Strain: 168 / JH642.
[5]	"Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis." Deutscher J., Reizer J., Fischer C., Galinier A., Saier M.H. Jr., Steinmetz M. J. Bacteriol. 176:3336-3344(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF SER-46.
[6]	"Specific recognition of the Bacillus subtilis gnt cis-acting catabolite-responsive element by a protein complex formed between CcpA and seryl-phosphorylated HPr." Fujita Y., Miwa Y., Galinier A., Deutscher J. Mol. Microbiol. 17:953-960(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis." Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M. Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-46, MASS SPECTROMETRY. Strain: 168.
[8]	"Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution." Herzberg O., Reddy P., Sutrina S., Saier M.H. Jr., Reizer J., Kapadia G. Proc. Natl. Acad. Sci. U.S.A. 89:2499-2503(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), PHOSPHORYLATION AT HIS-15.
[9]	"Refined structures of the active Ser83-->Cys and impaired Ser46-->Asp histidine-containing phosphocarrier proteins." Liao D.-I., Herzberg O. Structure 2:1203-1216(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS.
[10]	"Sequence-specific 1H NMR resonance assignments of Bacillus subtilis HPr: use of spectra obtained from mutants to resolve spectral overlap." Wittekind M., Reizer J., Klevit R.E. Biochemistry 29:7191-7200(1990) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[11]	"Solution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-dimensional NMR spectroscopy." Wittekind M., Rajagopal P., Branchini B.R., Reizer J., Saier M.H. Jr., Klevit R.E. Protein Sci. 1:1363-1376(1992) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[12]	"Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis." Jones B.E., Rajagopal P., Klevit R.E. Protein Sci. 6:2107-2119(1997) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[13]	"X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr." Fieulaine S., Morera S., Poncet S., Mijakovic I., Galinier A., Janin J., Deutscher J., Nessler S. Proc. Natl. Acad. Sci. U.S.A. 99:13437-13441(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 16-88 IN COMPLEX WITH L.CASEI HPRK/P.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X12832 Genomic DNA. Translation: CAA31317.1.
AL009126 Genomic DNA. Translation: CAB13263.1.

PIR

WQBSPH. S04177.

RefSeq

NP_389273.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JEM	NMR	-	A	2-88	[»]
1KKL	X-ray	2.80	H/I/J	1-88	[»]
1KKM	X-ray	2.80	H/I/J	1-88	[»]
1SPH	X-ray	2.00	A/B	1-88	[»]
2FEP	X-ray	2.45	S	2-87	[»]
2HID	NMR	-	A	2-88	[»]
2HPR	X-ray	2.00	A	2-88	[»]
3OQM	X-ray	2.96	D/S	2-88	[»]
3OQN	X-ray	3.30	D/S	2-88	[»]
3OQO	X-ray	2.97	D/S	2-88	[»]

ProteinModelPortal

P08877.

SMR

P08877. Positions 2-88.

ModBase

Search...

Protein-protein interaction databases

IntAct

P08877. 5 interactions.

STRING

224308.BSU13900.

PTM databases

PhosSite

P0802234.

Proteomic databases

PaxDb

P08877.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB13263; CAB13263; BSU13900.

GeneID

939259.

KEGG

bsu:BSU13900.

PATRIC

18974563. VBIBacSub10457_1473.

Organism-specific databases

GenoList

BSU13900. [Micado]

Phylogenomic databases

eggNOG

COG1925.

HOGENOM

HOG000278399.

KO

K11189.

OMA

SEIQLEY.

ProtClustDB

PRK13780.

Enzyme and pathway databases

BioCyc

BSUB:BSU13900-MONOMER.

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

P08877.

Entry information

Entry name

PTHP_BACSU

Accession

Primary (citable) accession number: P08877

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 142 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program