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P0AEC3 (ARCB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aerobic respiration control sensor protein ArcB

EC=2.7.13.3
Gene names
Name:arcB
Ordered Locus Names:b3210, JW5536
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length778 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Member of the two-component regulatory system ArcB/ArcA. Sensor-regulator protein for anaerobic repression of the arc modulon. Activates ArcA via a four-step phosphorelay. ArcB can also dephosphorylate ArcA by a reverse phosphorelay involving His-717 and Asp-576.

Catalytic activity

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.

Subcellular location

Cell inner membrane; Multi-pass membrane protein Ref.8.

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.

Sequence similarities

Contains 1 histidine kinase domain.

Contains 1 HPt domain.

Contains 1 PAC (PAS-associated C-terminal) domain.

Contains 1 PAS (PER-ARNT-SIM) domain.

Contains 1 response regulatory domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 778778Aerobic respiration control sensor protein ArcB
PRO_0000074684

Regions

Topological domain1 – 2525Cytoplasmic Potential
Transmembrane26 – 4621Helical; Potential
Topological domain47 – 5711Periplasmic Potential
Transmembrane58 – 7821Helical; Potential
Topological domain79 – 778700Cytoplasmic Potential
Domain153 – 22371PAS
Domain226 – 27853PAC
Domain289 – 507219Histidine kinase
Domain527 – 643117Response regulatory
Domain678 – 77194HPt

Amino acid modifications

Modified residue2921Phosphohistidine; by autocatalysis
Modified residue57614-aspartylphosphate Probable
Modified residue7171Phosphohistidine Probable

Experimental info

Mutagenesis2921H → Q: Loss of activity. Ref.7
Mutagenesis5761D → A: Loss of activity. Ref.7
Mutagenesis7171H → Q: Loss of activity. Ref.7
Sequence conflict469 – 4702Missing in AAA58012. Ref.2

Secondary structure

.................... 778
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AEC3 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: DD61EA6ECF95AD30

FASTA77887,983
        10         20         30         40         50         60 
MKQIRLLAQY YVDLMMKLGL VRFSMLLALA LVVLAIVVQM AVTMVLHGQV ESIDVIRSIF 

        70         80         90        100        110        120 
FGLLITPWAV YFLSVVVEQL EESRQRLSRL VQKLEEMRER DLSLNVQLKD NIAQLNQEIA 

       130        140        150        160        170        180 
VREKAEAELQ ETFGQLKIEI KEREETQIQL EQQSSFLRSF LDASPDLVFY RNEDKEFSGC 

       190        200        210        220        230        240 
NRAMELLTGK SEKQLVHLKP ADVYSPEAAA KVIETDEKVF RHNVSLTYEQ WLDYPDGRKA 

       250        260        270        280        290        300 
CFEIRKVPYY DRVGKRHGLM GFGRDITERK RYQDALERAS RDKTTFISTI SHELRTPLNG 

       310        320        330        340        350        360 
IVGLSRILLD TELTAEQEKY LKTIHVSAVT LGNIFNDIID MDKMERRKVQ LDNQPVDFTS 

       370        380        390        400        410        420 
FLADLENLSA LQAQQKGLRF NLEPTLPLPH QVITDGTRLR QILWNLISNA VKFTQQGQVT 

       430        440        450        460        470        480 
VRVRYDEGDM LHFEVEDSGI GIPQDELDKI FAMYYQVKDS HGGKPATGTG IGLAVSRRLA 

       490        500        510        520        530        540 
KNMGGDITVT SEQGKGSTFT LTIHAPSVAE EVDDAFDEDD MPLPALNVLL VEDIELNVIV 

       550        560        570        580        590        600 
ARSVLEKLGN SVDVAMTGKA ALEMFKPGEY DLVLLDIQLP DMTGLDISRE LTKRYPREDL 

       610        620        630        640        650        660 
PPLVALTANV LKDKQEYLNA GMDDVLSKPL SVPALTAMIK KFWDTQDDEE STVTTEENSK 

       670        680        690        700        710        720 
SEALLDIPML EQYLELVGPK LITDGLAVFE KMMPGYVSVL ESNLTAQDKK GIVEEGHKIK 

       730        740        750        760        770 
GAAGSVGLRH LQQLGQQIQS PDLPAWEDNV GEWIEEMKEE WRHDVEVLKA WVAKATKK 

« Hide

References

« Hide 'large scale' references
[1]"The arcB gene of Escherichia coli encodes a sensor-regulator protein for anaerobic repression of the arc modulon."
Iuchi S., Matsuda Z., Fujiwara T., Lin E.C.C.
Mol. Microbiol. 4:715-727(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Escherichia coli K-12: a cooperatively developed annotation snapshot -- 2005."
Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R., Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T., Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H., Thomson N.R., Wishart D., Wanner B.L.
Nucleic Acids Res. 34:1-9(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 469-470.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"In vitro phosphorylation study of the arc two-component signal transduction system of Escherichia coli."
Georgellis D., Lynch A.S., Lin E.C.C.
J. Bacteriol. 179:5429-5435(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: M15.
[6]"Signal decay through a reverse phosphorelay in the arc two-component signal transduction system."
Georgellis D., Kwon O., De Wulf P., Lin E.C.C.
J. Biol. Chem. 273:32864-32869(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: M15.
[7]"Phosphorelay as the sole physiological route of signal transmission by the arc two-component system of Escherichia coli."
Kwon O., Georgellis D., Lin E.C.C.
J. Bacteriol. 182:3858-3862(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-292; ASP-576 AND HIS-717.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[8]"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: K12 / MG1655 / ATCC 47076.
[9]"Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB."
Kato M., Mizuno T., Shimizu T., Hakoshima T.
Cell 88:717-723(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 660-778.
[10]"Crystallization of a complex between a novel C-terminal transmitter, HPt domain, of the anaerobic sensor kinase ArcB and the chemotaxis response regulator CheY."
Kato M., Mizuno T., Hakoshima T.
Acta Crystallogr. D 54:140-142(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 659-776 IN COMPLEX WITH CHEY.
[11]"Refined structure of the histidine-containing-phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB from Escherichia coli at 1.57-A resolution."
Kato M., Mizuno T., Shimizu T., Hakoshima T.
Acta Crystallogr. D 55:1842-1849(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 659-776.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53315 Genomic DNA. Translation: CAA37397.1.
U18997 Genomic DNA. Translation: AAA58012.1.
U00096 Genomic DNA. Translation: AAT48172.1.
AP009048 Genomic DNA. Translation: BAE77254.1.
PIRRGECAR. D65112.
RefSeqYP_026207.1. NC_000913.3.
YP_491395.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0BX-ray2.06A654-778[»]
1BDJX-ray2.68B654-778[»]
1FR0NMR-A654-778[»]
2A0BX-ray1.57A654-778[»]
2KSDNMR-A1-115[»]
ProteinModelPortalP0AEC3.
SMRP0AEC3. Positions 15-89, 276-646, 659-776.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47915N.
IntActP0AEC3. 7 interactions.
MINTMINT-98513.
STRING511145.b3210.

Proteomic databases

PaxDbP0AEC3.
PRIDEP0AEC3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT48172; AAT48172; b3210.
BAE77254; BAE77254; BAE77254.
GeneID12934428.
947887.
KEGGecj:Y75_p3130.
eco:b3210.
PATRIC32121840. VBIEscCol129921_3304.

Organism-specific databases

EchoBASEEB0060.
EcoGeneEG10062. arcB.

Phylogenomic databases

eggNOGCOG0642.
HOGENOMHOG000272667.
KOK07648.
OMAAPRLWQR.
OrthoDBEOG6G4VQG.
PhylomeDBP0AEC3.

Enzyme and pathway databases

BioCycEcoCyc:ARCB-MONOMER.
ECOL316407:JW5536-MONOMER.

Gene expression databases

GenevestigatorP0AEC3.

Family and domain databases

Gene3D1.10.287.130. 1 hit.
1.10.287.970. 1 hit.
1.20.120.160. 1 hit.
3.30.565.10. 1 hit.
InterProIPR027460. ArcB_TM.
IPR011006. CheY-like_superfamily.
IPR003661. EnvZ-like_dim/P.
IPR003594. HATPase_ATP-bd.
IPR000014. PAS.
IPR000700. PAS-assoc_C.
IPR013767. PAS_fold.
IPR004358. Sig_transdc_His_kin-like_C.
IPR008207. Sig_transdc_His_kin_Hpt_dom.
IPR014409. Sig_transdc_His_kin_hyb_ArcB.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamPF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF01627. Hpt. 1 hit.
PF00989. PAS. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PIRSFPIRSF003182. ArcB. 1 hit.
PRINTSPR00344. BCTRLSENSOR.
SMARTSM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00073. HPT. 1 hit.
SM00091. PAS. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMSSF47226. SSF47226. 1 hit.
SSF47384. SSF47384. 1 hit.
SSF52172. SSF52172. 1 hit.
SSF55785. SSF55785. 1 hit.
SSF55874. SSF55874. 1 hit.
TIGRFAMsTIGR00229. sensory_box. 1 hit.
PROSITEPS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
PS50113. PAC. 1 hit.
PS50112. PAS. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AEC3.
PROP0AEC3.

Entry information

Entry nameARCB_ECOLI
AccessionPrimary (citable) accession number: P0AEC3
Secondary accession number(s): P22763, Q2M902
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: June 11, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene