Aerobic respiration control sensor protein ArcB - Escherichia coli (strain K12)

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P0AEC3 (ARCB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 83. History...

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

Documents (3) |

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:
Aerobic respiration control sensor protein ArcB
EC=2.7.13.3

Gene names

Name:	arcB
Ordered Locus Names:	b3210, JW5536

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	778 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

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 Reference proteome
Gene Ontology (GO)
Biological_process	intracellular signal transduction Inferred from electronic annotation. Source: GOC protein autophosphorylation Inferred from mutant phenotype PubMed 20097862. Source: CACAO 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 direct assay Ref.1. Source: EcoCyc plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW histidine phosphotransfer kinase activity Inferred from direct assay PubMed 1512197. Source: EcoCyc phosphorelay response regulator activity Inferred from electronic annotation. Source: InterPro phosphorelay sensor kinase activity Inferred from direct assay PubMed 1512197. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 778

778

Aerobic respiration control sensor protein ArcB

PRO_0000074684

Regions

Topological domain

1 – 25

Cytoplasmic Potential

Transmembrane

26 – 46

Helical; Potential

Topological domain

47 – 57

Periplasmic Potential

Transmembrane

58 – 78

Helical; Potential

Topological domain

79 – 778

700

Cytoplasmic Potential

Domain

153 – 223

PAS

Domain

226 – 278

PAC

Domain

289 – 507

219

Histidine kinase

Domain

527 – 643

117

Response regulatory

Domain

678 – 771

HPt

Amino acid modifications

Modified residue

292

Phosphohistidine; by autocatalysis

Modified residue

576

4-aspartylphosphate Probable

Modified residue

717

Phosphohistidine Probable

Experimental info

Mutagenesis

292

H → Q: Loss of activity. Ref.7

Mutagenesis

576

D → A: Loss of activity. Ref.7

Mutagenesis

717

H → Q: Loss of activity. Ref.7

Sequence conflict

469 – 470

Missing in AAA58012. Ref.2

Secondary structure

778

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AEC3 [UniParc].

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

FASTA

778

87,983

        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' referencesShow '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 277:1453-1474(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.

PIR

RGECAR. D65112.

RefSeq

YP_026207.1. NC_000913.2.
YP_491395.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A0B	X-ray	2.06	A	654-778	[»]
1BDJ	X-ray	2.68	B	654-778	[»]
1FR0	NMR	-	A	654-778	[»]
2A0B	X-ray	1.57	A	654-778	[»]
2KSD	NMR	-	A	1-115	[»]

ProteinModelPortal

P0AEC3.

SMR

P0AEC3. Positions 15-89, 277-503, 528-646, 659-776.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47915N.

IntAct

P0AEC3. 5 interactions.

MINT

MINT-98513.

STRING

511145.b3210.

Proteomic databases

PaxDb

P0AEC3.

PRIDE

P0AEC3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAT48172; AAT48172; b3210.
BAE77254; BAE77254; BAE77254.

GeneID

12934428.
947887.

KEGG

ecj:Y75_p3130.
eco:b3210.

PATRIC

32121840. VBIEscCol129921_3304.

Organism-specific databases

EchoBASE

EB0060.

EcoGene

EG10062. arcB.

Phylogenomic databases

eggNOG

COG0642.

HOGENOM

HOG000272667.

K07648.

OMA

ESRNLEN.

OrthoDB

EOG6G4VQG.

ProtClustDB

PRK11091.

Enzyme and pathway databases

BioCyc

EcoCyc:ARCB-MONOMER.
ECOL316407:JW5536-MONOMER.

Gene expression databases

Genevestigator

P0AEC3.

Family and domain databases

Gene3D

1.10.287.130. 1 hit.
1.10.287.970. 1 hit.
1.20.120.160. 1 hit.
3.30.565.10. 1 hit.

InterPro

IPR027460. 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]

Pfam

PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF01627. Hpt. 1 hit.
PF00989. PAS. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]

PIRSF

PIRSF003182. ArcB. 1 hit.

PRINTS

PR00344. BCTRLSENSOR.

SMART

SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00073. HPT. 1 hit.
SM00091. PAS. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]

SUPFAM

SSF47226. SSF47226. 1 hit.
SSF47384. SSF47384. 1 hit.
SSF52172. SSF52172. 1 hit.
SSF55785. SSF55785. 1 hit.
SSF55874. SSF55874. 1 hit.

TIGRFAMs

TIGR00229. sensory_box. 1 hit.

PROSITE

PS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
PS50113. PAC. 1 hit.
PS50112. PAS. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0AEC3.

PRO

P0AEC3.

Entry information

Entry name

ARCB_ECOLI

Accession

Primary (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:	November 13, 2013
This is version 83 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

Escherichia coli

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

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

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents