![]() | extracellular side |
cytoplasmic side |
MOTB_ECOLI » Motility protein B » Chemotaxis protein MotB; | |
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Hydrophobic Thickness | 30.4 ± 3.0 Å |
Tilt Angle | 14 ± 11° |
ΔGtransfer | -21.9 kcal/mol |
ΔGfold | -17.8 kcal/mol |
Links | UniProtKB, Pfam, Interpro, iHOP, STRING |
Topology | In |
TM Segments | 26-48 (21-50) |
Pathways | Bacterial chemotaxis (KEGG) Flagellar assembly (KEGG) |
PDB | none |
OPM | none |
Complexes | |
Interactions | |
Domains | AA: 11-66, Membrane MotB of proton-channel complex MotA/MotB AA: 160-259, PDBID: 2ZOV, Subunit A, Seq Identity:80%, OmpA family |
UniProt annotation for MOTB_ECOLI » Motility protein B |
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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. SUBUNIT: 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. |
UniProt features for MOTB_ECOLI » Motility protein B |
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CHAIN 1 308 Motility protein B. DOMAIN 148 268 OmpA-like. |
Amino Acid Sequence for MOTB_ECOLI » Motility protein B |
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MKNQAHPIIV VKRRKAKSHG AAHGSWKIAY ADFMTAMMAF FLVMWLISIS SPKELIQIAE YFRTPLATAV TGGDRISNSE SPIPGGGDDY TQSQGEVNKQ PNIEELKKRM EQSRLRKLRG DLDQLIESDP KLRALRPHLK IDLVQEGLRI QIIDSQNRPM FRTGSADVEP YMRDILRAIA PVLNGIPNRI SLSGHTDDFP YASGEKGYSN WELSADRANA SRRELMVGGL DSGKVLRVVG MAATMRLSDR GPDDAVNRRI SLLVLNKQAE QAILHENAES QNEPVSALEK PEVAPQVSVP TMPSAEPR |