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P0AF06 (MOTB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Motility protein B
Alternative name(s):
Chemotaxis protein MotB
Gene names
Name:motB
Ordered Locus Names:b1889, JW1878
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length308 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Probably a linker that fastens the torque-generating machinery to the cell wall. Overexpression of this protein with MotA improves motility in a yhjH disruption, (a c-di-GMP phosphodiesterase) suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein YcgR and the flagellar stator. Ref.8

Subunit structure

Each stator complex is composed of 4 MotA and 2 MotB subunits; in E.coli 11 to 12 stator complexes can be involved in flagellar rotation. 2 A subunits and 1 B subunit are thought to form a single ion channel, so that each stator complex contains two channels.

Subcellular location

Cell inner membrane; Single-pass type II membrane protein. Note: The OmpA-like domain probably functions to anchor the complex to the cell wall. Ref.6

Sequence similarities

Belongs to the MotB family.

Contains 1 OmpA-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 308308Motility protein B
PRO_0000189585

Regions

Topological domain1 – 2727Cytoplasmic Probable
Transmembrane28 – 4922Helical; Signal-anchor for type II membrane protein; Probable
Topological domain50 – 308259Periplasmic Probable
Domain148 – 268121OmpA-like

Experimental info

Mutagenesis311A → T: Complete loss of motility.
Mutagenesis321D → N: Complete loss of motility. Ref.7
Mutagenesis391A → V: Complete loss of motility. Ref.7
Mutagenesis1591P → I: Decreased motility, subnormal torque, tethered strains rotate very slowly. Ref.7
Mutagenesis1641G → D: Complete loss of motility. Ref.7
Mutagenesis1961T → I: Complete loss of motility. Ref.7
Mutagenesis1971D → N: Complete loss of motility. Ref.7
Mutagenesis2051E → K: Decreased motility, subnormal torque, tethered strains rotate very slowly, maybe reduced affinity for the motor. Ref.7
Mutagenesis2141S → F: Complete loss of motility. Ref.7
Mutagenesis2171R → W: Complete loss of motility. Ref.7
Mutagenesis2221R → H: Complete loss of motility. Ref.7
Mutagenesis2401G → D: Decreased motility, subnormal torque, tethered strains rotate very slowly. Ref.7
Mutagenesis2421A → T or V: Complete loss of motility. Ref.7
Mutagenesis2581R → C or H: Complete loss of motility. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P0AF06 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 2F20C551C44BD6E3

FASTA30834,186
        10         20         30         40         50         60 
MKNQAHPIIV VKRRKAKSHG AAHGSWKIAY ADFMTAMMAF FLVMWLISIS SPKELIQIAE 

        70         80         90        100        110        120 
YFRTPLATAV TGGDRISNSE SPIPGGGDDY TQSQGEVNKQ PNIEELKKRM EQSRLRKLRG 

       130        140        150        160        170        180 
DLDQLIESDP KLRALRPHLK IDLVQEGLRI QIIDSQNRPM FRTGSADVEP YMRDILRAIA 

       190        200        210        220        230        240 
PVLNGIPNRI SLSGHTDDFP YASGEKGYSN WELSADRANA SRRELMVGGL DSGKVLRVVG 

       250        260        270        280        290        300 
MAATMRLSDR GPDDAVNRRI SLLVLNKQAE QAILHENAES QNEPVSALEK PEVAPQVSVP 


TMPSAEPR 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the Escherichia coli motB gene and site-limited incorporation of its product into the cytoplasmic membrane."
Stader J., Matsumura P., Vacante D., Dean G.E., Macnab R.M.
J. Bacteriol. 166:244-252(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"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.
[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]"Tandem translation starts in the cheA locus of Escherichia coli."
Kofoid E.C., Parkinson J.S.
J. Bacteriol. 173:2116-2119(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 276-308.
[6]"Bacterial motility: membrane topology of the Escherichia coli MotB protein."
Chun S.Y., Parkinson J.S.
Science 239:276-278(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TOPOLOGY, SUGGESTION OF ROLE AS A CELL-WALL ANCHOR.
[7]"Mutant MotB proteins in Escherichia coli."
Blair D.F., Kim D.Y., Berg H.C.
J. Bacteriol. 173:4049-4055(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-32; ALA-39; PRO-159; GLY-164; THE-196; ASP-197; GLU-205; SER-214; ARG-217; ARG-222; GLY-240; ALA-242 AND ARG-258.
Strain: K12 / RP437.
[8]"The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a 'backstop brake' mechanism."
Paul K., Nieto V., Carlquist W.C., Blair D.F., Harshey R.M.
Mol. Cell 38:128-139(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: K12 / RP3098.
[9]"Flagellar motility in bacteria structure and function of flagellar motor."
Terashima H., Kojima S., Homma M.
Int. Rev. Cytol. 270:39-85(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01652 Genomic DNA. Translation: AAA24178.1.
U00096 Genomic DNA. Translation: AAC74959.1.
AP009048 Genomic DNA. Translation: BAA15710.1.
M34669 Genomic DNA. Translation: AAA23572.1.
PIRQRECMB. A64952.
RefSeqNP_416403.1. NC_000913.3.
YP_490151.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0AF06.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47996N.
IntActP0AF06. 4 interactions.
STRING511145.b1889.

Protein family/group databases

TCDB1.A.30.1.1. the h(+)- or na(+)-translocating bacterial flagellar motor/exbbd outer membrane transport energizer (mot/exb) superfamily.

Proteomic databases

PaxDbP0AF06.
PRIDEP0AF06.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74959; AAC74959; b1889.
BAA15710; BAA15710; BAA15710.
GeneID12932041.
946402.
KEGGecj:Y75_p1865.
eco:b1889.
PATRIC32119105. VBIEscCol129921_1970.

Organism-specific databases

EchoBASEEB0597.
EcoGeneEG10602. motB.

Phylogenomic databases

eggNOGCOG1360.
HOGENOMHOG000254689.
KOK02557.
OMAQDGLRIQ.
OrthoDBEOG6VQPR8.
PhylomeDBP0AF06.

Enzyme and pathway databases

BioCycEcoCyc:MOTB-FLAGELLAR-MOTOR-STATOR-PROTEIN.
ECOL316407:JW1878-MONOMER.

Gene expression databases

GenevestigatorP0AF06.

Family and domain databases

Gene3D3.30.1330.60. 1 hit.
InterProIPR025713. MotB_N_dom.
IPR006665. OmpA/MotB_C.
[Graphical view]
PfamPF13677. MotB_plug. 1 hit.
PF00691. OmpA. 1 hit.
[Graphical view]
SUPFAMSSF103088. SSF103088. 1 hit.
PROSITEPS51123. OMPA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP0AF06.

Entry information

Entry nameMOTB_ECOLI
AccessionPrimary (citable) accession number: P0AF06
Secondary accession number(s): P09349
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: June 11, 2014
This is version 77 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

Escherichia coli

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