UniProt Accession

 HIPA_ECOLI; P23874; P76139; P76880; P77507 

Genbank Protein ID

 M61242; U00096; AP009048 

Genbank Nucleotide ID

 AAA56878.1; AAC74580.1; BAA15179.2 

Protein Name

 Serine/threonine-protein kinase HipA 

Protein Synonyms/Alias

 Ser/Thr-protein kinase HipA; Toxin HipA 

Gene Name

 hipA 

Gene Synonyms/Alias

 b1507; JW1500 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
18	QRVGELTKLANGAHT	acetylation	[1]
27	ANGAHTFKYAPEWLA	acetylation	[1]
363	LNASKGKKTAIDKIY	acetylation	[1]
368	GKKTAIDKIYPRHFL	acetylation	[1]
379	RHFLATAKVLRFPEV	acetylation	[1]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 

Functional Description

 Toxic component of a toxin-antitoxin (TA) module. Autophosphorylates (Ser-150) and phosphorylates EF-Tu in vitro (on 'Thr-383'), may act on other proteins as well. The hipA7 mutation leads to increased generation of persister cells, cells that survive antibiotic treatment probably by entering into a dormant state. Wild-type cells produce persisters at a frequency of 10-6 to 10-5 whereas mutant hipA7 cells produce persisters at a frequency of 10-2. Generation of persister cells requires (p)ppGpp as cells lacking relA or relA/spoT generate fewer or no persister cells respectively compared to hipA7. Low level expression of HipA causes cell filamentation and depending on the protein level is toxic enough to reduce cell growth or even kill cells. Expression of wild-type HipA also leads to high antibiotic tolerance of the survivor cells. The toxic effect of HipA is neutralized by its cognate antitoxin HipB. With HipB acts as a corepressor for transcription of the hipBA promoter. 

Sequence Annotation

 NP_BIND 152 157 ATP.
 NP_BIND 234 236 ATP.
 NP_BIND 311 314 ATP.
 NP_BIND 331 332 ATP.
 ACT_SITE 309 309 Proton acceptor (Probable).
 METAL 314 314 Magnesium 1.
 METAL 332 332 Magnesium 1.
 METAL 332 332 Magnesium 2.
 BINDING 181 181 ATP.
 MOD_RES 150 150 Phosphoserine; by autocatalysis.  

Keyword

 3D-structure; ATP-binding; Complete proteome; Direct protein sequencing; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; Repressor; Serine/threonine-protein kinase; Toxin; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 440 AA 

Protein Sequence

Gene Ontology

 GO:0005524; F:ATP binding; IDA:EcoCyc.
 GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:EcoCyc.
 GO:0022611; P:dormancy process; IDA:EcoCyc. 

Interpro

 IPR012893; HipA-like_C.
 IPR012894; HipA-like_N.
 IPR017508; HipA_N. 

Pfam

 PF07804; HipA_C
 PF07805; HipA_N 

SMART

  

PROSITE

  

PRINTS