Signal transduction histidine-protein kinase BarA

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P0AEC6 (BARA_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 58. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Signal transduction histidine-protein kinase BarA
EC=2.7.13.3

Gene names

Name:	barA
Ordered Locus Names:	c3349

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	918 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Member of the two-component regulatory system UvrY/BarA involved in the regulation of carbon metabolism via the CsrA/CsrB regulatory system. Phosphorylates UvrY, probably via a four-step phosphorelay By similarity.
Catalytic activity	ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Subcellular location	Cell inner membrane; Multi-pass membrane protein By similarity.
Post-translational modification	Activation requires a sequential transfer of a phosphate group from a His in the primary transmitter domain, to an Asp in the receiver domain and to a His in the secondary transmitter domain By similarity.
Sequence similarities	Contains 1 HAMP domain. Contains 1 histidine kinase domain. Contains 1 HPt domain. Contains 1 response regulatory domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Two-component regulatory system
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	peptidyl-histidine phosphorylation Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW two-component response regulator activity Inferred from electronic annotation. Source: InterPro two-component sensor 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 – 918

918

Signal transduction histidine-protein kinase BarA

PRO_0000074699

Regions

Topological domain

1 – 9

Cytoplasmic Potential

Transmembrane

10 – 31

Helical; Potential

Topological domain

32 – 176

145

Periplasmic Potential

Transmembrane

177 – 196

Helical; Potential

Topological domain

197 – 918

722

Cytoplasmic Potential

Domain

200 – 252

HAMP

Domain

299 – 520

222

Histidine kinase

Domain

669 – 785

117

Response regulatory

Domain

822 – 918

HPt

Amino acid modifications

Modified residue

302

Phosphohistidine; by autocatalysis By similarity

Modified residue

718

4-aspartylphosphate By similarity

Modified residue

861

Phosphohistidine By similarity

Secondary structure

918

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AEC6 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: EA31D6D732F023CD
Show »

FASTA

918

102,453

        10         20         30         40         50         60 
MTNYSLRARM MILILAPTVL IGLLLSIFFV VHRYNDLQRQ LEDAGASIIE PLAVSTEYGM 

        70         80         90        100        110        120 
SLQNRESIGQ LISVLHRRHS DIVRAISVYD ENNRLFVTSN FHLDPSSMQL GSNVPFPRQL 

       130        140        150        160        170        180 
TVTRDGDIMI LRTPIISESY SPDESPSSDA KNSQNMLGYI ALELDLKSVR LQQYKEIFIS 

       190        200        210        220        230        240 
SVMMLFCIGI ALIFGWRLMR DVTGPIRNMV NTVDRIRRGQ LDSRVEGFML GELDMLKNGI 

       250        260        270        280        290        300 
NSMAMSLAAY HEEMQHNIDQ ATSDLRETLE QMEIQNVELD LAKKRAQEAA RIKSEFLANM 

       310        320        330        340        350        360 
SHELRTPLNG VIGFTRLTLK TELTPTQRDH LNTIERSANN LLAIINDVLD FSKLEAGKLI 

       370        380        390        400        410        420 
LESIPFPLRS TLDEVVTLLA HSSHDKGLEL TLNIKSDVPD NVIGDPLRLQ QIITNLVGNA 

       430        440        450        460        470        480 
IKFTENGNID ILVEKRALSN TKVQIEVQIR DTGIGIPERD QSRLFQAFRQ ADASISRRHG 

       490        500        510        520        530        540 
GTGLGLVITQ KLVNEMGGDI SFHSQPNRGS TFWFHINLDL NPNIIIEGPS TQCLAGKRLA 

       550        560        570        580        590        600 
YVEPNSAAAQ CTLDILSETP LEVVYSPTFS ALPPAHYDMM LLGIAVTFRE PLTMQHERLA 

       610        620        630        640        650        660 
KAVSMTDFLM LALPCHAQVN AEKLKQDGIG ACLLKPLTPT RLLPALTEFC HHKQNTLLPV 

       670        680        690        700        710        720 
TDESKLAMTV MAVDDNPANL KLIGALLEDM VQHVELCDSG HQAVERAKQM PFDLILMDIQ 

       730        740        750        760        770        780 
MPDMDGIRAC ELIHQLPHQQ QTPVIAVTAH AMAGQKEKLL GAGMSDYLAK PIEEERLHNL 

       790        800        810        820        830        840 
LLRYKPGSGI SSRVVTPEVN EIVVNPNATL DWQLALRQAA GKTDLARDML QMLLDFLPEV 

       850        860        870        880        890        900 
RNKVEEQLVG ENPEGLVDLI HKLHGSCGYS GVPRMKNLCQ LIEQQLRSGT KEEDLEPELL 

       910 
ELLDEMDNVA REASKILG

« Hide

References

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE014075 Genomic DNA. Translation: AAN81797.1.

RefSeq

NP_755227.1. NC_004431.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3IQT	X-ray	1.40	A	799-918	[»]

ProteinModelPortal

P0AEC6.

SMR

P0AEC6. Positions 200-250, 285-519, 531-787, 799-918.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000045429; EBESCP00000043778; EBESCG00000044479.

GeneID

1039190.

GenomeReviews

Gene locus c3349 in contig AE014075_GR.

KEGG

ecc:c3349.

PATRIC

18284530. VBIEscCol75197_3154.

Organism-specific databases

CMR

Search...

Phylogenomic databases

GeneTree

EBGT00070000031695.

HOGENOM

HBG298668.

OMA

VESAANQ.

PhylomeDB

P0AEC6.

ProtClustDB

PRK11107.

Family and domain databases

InterPro

IPR003594. ATPase-like_ATP-bd.
IPR011006. CheY-like_superfamily.
IPR003660. HAMP_linker_domain.
IPR019247. Histidine_kinase_BarA_N.
IPR004358. Sig_transdc_His_kin-like_C.
IPR008207. Sig_transdc_His_kin_Hpt_dom.
IPR003661. Sig_transdc_His_kin_sub1_dim/P.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]

Gene3D

G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
G3DSA:1.20.120.160. Sig_transdc_His_kin_Hpt_dom. 1 hit.

K07678.

Pfam

PF09984. DUF2222. 1 hit.
PF00672. HAMP. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF01627. Hpt. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]

PRINTS

PR00344. BCTRLSENSOR.

SMART

SM00304. HAMP. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00073. HPT. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]

SUPFAM

SSF55874. ATP_bd_ATPase. 1 hit.
SSF52172. CheY_like. 1 hit.
SSF47384. His_kin_homodim. 1 hit.
SSF47226. Hpt. 1 hit.

PROSITE

PS50885. HAMP. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

BARA_ECOL6

Accession

Primary (citable) accession number: P0AEC6
Secondary accession number(s): P26607, P77032

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 6, 2005
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents