MOTB_ECOLI » Motility protein B

MOTB_ECOLI » Motility protein B
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Topology in Bacterial Gram-negative inner membrane
Topologyextracellular side
cytoplasmic side
MOTB_ECOLI » Motility protein B » Chemotaxis protein MotB;
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

MOTB:MOTB_SALTY

MOTB:MOTB_HELPY

Interactions

MOTB, Complex: Homodimer of motility protein B, PDBID: 2ZVY
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
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
CHAIN 1 308 Motility protein B.
DOMAIN 148 268 OmpA-like.
Amino Acid Sequence for MOTB_ECOLI » Motility protein B
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