hipA:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

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Standard name

HipA

Synonyms

regulator with hipB[1], B1507[2][1], HipA[2][1] , ECK1500, JW1500, b1507

Product description

HipA Polypeptide[2]; serine kinase HipA[3];

Component of HipB transcriptional repressor[3]

Toxin, growth inhibition blocked by continuous HipB synthesis;; probable role in cell division[4]

EC number (for enzymes)


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Notes

Function

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<protect> Gene Ontology
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Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

Subunits of HipB transcriptional repressor

could be indirect

Protein

tehB

PMID:19402753[5]

MALDI(Z-score):29.262247

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Notes

Localization

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Compartment Description Evidence Reference/Source Notes
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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc 

MPKLVTWMNN QRVGELTKLA NGAHTFKYAP EWLASRYARP LSLSLPLQRG NITSDAVFNF
FDNLLPDSPI VRDRIVKRYH AKSRQPFDLL SEIGRDSVGA VTLIPEDETV THPIMAWEKL
TEARLEEVLT AYKADIPLGM IREENDFRIS VAGAQEKTAL LRIGNDWCIP KGITPTTHII
KLPIGEIRQP NATLDLSQSV DNEYYCLLLA KELGLNVPDA EIIKAGNVRA LAVERFDRRW
NAERTVLLRL PQEDMCQTFG LPSSVKYESD GGPGIARIMA FLMGSSEALK DRYDFMKFQV
FQWLIGATDG HAKNFSVFIQ AGGSYRLTPF YDIISAFPVL GGTGIHISDL KLAMGLNASK
GKKTAIDKIY PRHFLATAKV LRFPEVQMHE ILSDFARMIP AALDNVKTSL PTDFPENVVT
AVESNVLRLH GRLSREYGSK
Length

440

Mol. Wt

49.277 kDa

pI

8.3 (calculated)

Extinction coefficient

50,880 - 51,255 (calc based on 12 Y, 6 W, and 3 C residues)

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Domains/Motifs/Modification Sites

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Type Residues Description Notes References

Modification Site

150

phosphorylation site at S150

probability greater than 75%

PMID:17938405[6]

Domain

249..332

PF07804 HipA-like C-terminal domain

PMID:19920124[7]

Domain

150..238

PF07805 HipA-like N-terminal domain

PMID:19920124[7]

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Structure
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Structures

<beststructure> gene=hipA taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16129466

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:946064

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0005022

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P23874

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10443

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10443

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:946064

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000436

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0438

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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

  1. ↑ 1.0 1.1 1.2 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  6. ↑ Macek, B et al. (2008) Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol. Cell Proteomics 7 299-307 PubMed
  7. ↑ 7.0 7.1 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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