ECOLI:HIPA

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	hipA
Protein Name(s)	Serine/threonine-protein kinase HipA Ser/Thr-protein kinase HipA Toxin HipA
External Links
UniProt	P23874
EMBL	M61242 U00096 AP009048
PIR	F64904
RefSeq	NP_416024.1 YP_489771.1
PDB	2WIU 3DNT 3DNU 3DNV 3FBR 3HZI 3TPB 3TPD 3TPE 3TPT 3TPV
PDBsum	2WIU 3DNT 3DNU 3DNV 3FBR 3HZI 3TPB 3TPD 3TPE 3TPT 3TPV
ProteinModelPortal	P23874
SMR	P23874
DIP	DIP-9898N
IntAct	P23874
MINT	MINT-1292260
STRING	511145.b1507
PhosSite	P0612176
PaxDb	P23874
PRIDE	P23874
EnsemblBacteria	AAC74580 BAA15179
GeneID	12931226 946064
KEGG	ecj:Y75_p1482 eco:b1507
PATRIC	32118308
EchoBASE	EB0438
EcoGene	EG10443
eggNOG	COG3550
HOGENOM	HOG000188799
InParanoid	P23874
KO	K07154
OMA	SCENEWL
OrthoDB	EOG6ZSP44
BioCyc	EcoCyc:EG10443-MONOMER ECOL316407:JW1500-MONOMER MetaCyc:EG10443-MONOMER
EvolutionaryTrace	P23874
PRO	PR:P23874
Proteomes	UP000000318 UP000000625
Genevestigator	P23874
GO	GO:0005524 GO:0003677 GO:0000287 GO:0004674 GO:0022611 GO:0043086 GO:0036289 GO:0046677 GO:0044010
InterPro	IPR012893 IPR017508 IPR012894
Pfam	PF13657 PF07804 PF07805
TIGRFAMs	TIGR03071

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0016301	kinase activity	PMID:19150849^[1]	ECO:0000314			F	Figure 1 shows the structure of the hipA protein, including its binding domains. Figure 1d shows the hipA kinase assay using EF-Tu as a substrate (immunoblot).	complete
enables	GO:0043565	sequence-specific DNA binding	PMID:19150849^[1]	ECO:0005670	x-ray crystallography evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0032993	protein-DNA complex	PMID:19150849^[1]	ECO:0005670	x-ray crystallography evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0032993	protein-DNA complex	PMID:8021189^[2]	ECO:0005631	DNAse footprinting evidence used in manual assertion	RefSeq:NC_012892.2	C	Seeded From UniProt	complete
part_of	GO:0032993	protein-DNA complex	PMID:8021189^[2]	ECO:0001807	electrophoretic mobility shift assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0001217	DNA-binding transcription repressor activity	PMID:8021189^[2]	ECO:0005631	DNAse footprinting evidence used in manual assertion	RefSeq:NC_012892.2	F	Seeded From UniProt	complete
enables	GO:0001217	DNA-binding transcription repressor activity	PMID:8021189^[2]	ECO:0001807	electrophoretic mobility shift assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000976	transcription regulatory region sequence-specific DNA binding	PMID:8021189^[2]	ECO:0005631	DNAse footprinting evidence used in manual assertion	RefSeq:NC_012892.2	F	Seeded From UniProt	complete
enables	GO:0000976	transcription regulatory region sequence-specific DNA binding	PMID:8021189^[2]	ECO:0001807	electrophoretic mobility shift assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10443 PANTHER:PTN002205379	C	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10443 PANTHER:PTN002205379	F	Seeded From UniProt	complete
involved_in	GO:0044010	single-species biofilm formation	PMID:23329678^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0043086	negative regulation of catalytic activity	PMID:24095282^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0036289	peptidyl-serine autophosphorylation	PMID:17041039^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0022611	dormancy process	PMID:16707675^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:19150849^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:17041039^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:19150849^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0001217	P	Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0001217	P	Seeded From UniProt	complete
involved_in	GO:0046677	response to antibiotic	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0046	P	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F	Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0723	F	Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	F	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 Schumacher, MA et al. (2009) Molecular mechanisms of HipA-mediated multidrug tolerance and its neutralization by HipB. Science 323 396-401 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Black, DS et al. (1994) Autoregulation of hip, an operon that affects lethality due to inhibition of peptidoglycan or DNA synthesis. J. Bacteriol. 176 4081-91 PubMed GONUTS page
↑ ^3.0 ^3.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Zhao, J et al. (2013) Escherichia coli toxin gene hipA affects biofilm formation and DNA release. Microbiology (Reading, Engl.) 159 633-40 PubMed GONUTS page
↑ Germain, E et al. (2013) Molecular mechanism of bacterial persistence by HipA. Mol. Cell 52 248-54 PubMed GONUTS page
↑ ^6.0 ^6.1 Correia, FF et al. (2006) Kinase activity of overexpressed HipA is required for growth arrest and multidrug tolerance in Escherichia coli. J. Bacteriol. 188 8360-7 PubMed GONUTS page
↑ Korch, SB & Hill, TM (2006) Ectopic overexpression of wild-type and mutant hipA genes in Escherichia coli: effects on macromolecular synthesis and persister formation. J. Bacteriol. 188 3826-36 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:19150849-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 Schumacher, MA et al. (2009) Molecular mechanisms of HipA-mediated multidrug tolerance and its neutralization by HipB. Science 323 396-401 PubMed GONUTS page

[PMID:8021189-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Black, DS et al. (1994) Autoregulation of hip, an operon that affects lethality due to inhibition of peptidoglycan or DNA synthesis. J. Bacteriol. 176 4081-91 PubMed GONUTS page

[PMID:21873635-3] 3.0 ^3.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:23329678-4] Zhao, J et al. (2013) Escherichia coli toxin gene hipA affects biofilm formation and DNA release. Microbiology (Reading, Engl.) 159 633-40 PubMed GONUTS page

[PMID:24095282-5] Germain, E et al. (2013) Molecular mechanism of bacterial persistence by HipA. Mol. Cell 52 248-54 PubMed GONUTS page

[PMID:17041039-6] 6.0 ^6.1 Correia, FF et al. (2006) Kinase activity of overexpressed HipA is required for growth arrest and multidrug tolerance in Escherichia coli. J. Bacteriol. 188 8360-7 PubMed GONUTS page

[PMID:16707675-7] Korch, SB & Hill, TM (2006) Ectopic overexpression of wild-type and mutant hipA genes in Escherichia coli: effects on macromolecular synthesis and persister formation. J. Bacteriol. 188 3826-36 PubMed GONUTS page

[PMID:18304323-8] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

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ECOLI:HIPA

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