MOTB_ECOLI
ID MOTB_ECOLI Reviewed; 308 AA.
AC P0AF06; P09349;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Motility protein B;
DE AltName: Full=Chemotaxis protein MotB;
GN Name=motB; OrderedLocusNames=b1889, JW1878;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3007435; DOI=10.1128/jb.166.1.244-252.1986;
RA Stader J., Matsumura P., Vacante D., Dean G.E., Macnab R.M.;
RT "Nucleotide sequence of the Escherichia coli motB gene and site-limited
RT incorporation of its product into the cytoplasmic membrane.";
RL J. Bacteriol. 166:244-252(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 276-308.
RX PubMed=2002011; DOI=10.1128/jb.173.6.2116-2119.1991;
RA Kofoid E.C., Parkinson J.S.;
RT "Tandem translation starts in the cheA locus of Escherichia coli.";
RL J. Bacteriol. 173:2116-2119(1991).
RN [6]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND SUGGESTION OF ROLE AS A CELL-WALL
RP ANCHOR.
RX PubMed=2447650; DOI=10.1126/science.2447650;
RA Chun S.Y., Parkinson J.S.;
RT "Bacterial motility: membrane topology of the Escherichia coli MotB
RT protein.";
RL Science 239:276-278(1988).
RN [7]
RP MUTAGENESIS OF ASP-32; ALA-39; PRO-159; GLY-164; THR-196; ASP-197; GLU-205;
RP SER-214; ARG-217; ARG-222; GLY-240; ALA-242 AND ARG-258.
RC STRAIN=K12 / RP437;
RX PubMed=2061285; DOI=10.1128/jb.173.13.4049-4055.1991;
RA Blair D.F., Kim D.Y., Berg H.C.;
RT "Mutant MotB proteins in Escherichia coli.";
RL J. Bacteriol. 173:4049-4055(1991).
RN [8]
RP FUNCTION.
RC STRAIN=K12 / RP3098;
RX PubMed=20346719; DOI=10.1016/j.molcel.2010.03.001;
RA Paul K., Nieto V., Carlquist W.C., Blair D.F., Harshey R.M.;
RT "The c-di-GMP binding protein YcgR controls flagellar motor direction and
RT speed to affect chemotaxis by a 'backstop brake' mechanism.";
RL Mol. Cell 38:128-139(2010).
RN [9]
RP REVIEW.
RX PubMed=19081534; DOI=10.1016/s1937-6448(08)01402-0;
RA Terashima H., Kojima S., Homma M.;
RT "Flagellar motility in bacteria structure and function of flagellar
RT motor.";
RL Int. Rev. Cytol. 270:39-85(2008).
CC -!- FUNCTION: MotA and MotB comprise the stator element of the flagellar
CC motor complex. Required for the rotation of the flagellar motor.
CC Probably a linker that fastens the torque-generating machinery to the
CC cell wall. Overexpression of this protein with MotA improves motility
CC in a pdeH disruption, (a c-di-GMP phosphodiesterase) suggesting there
CC is an interaction (direct or indirect) between the c-di-GMP-binding
CC flagellar brake protein YcgR and the flagellar stator.
CC {ECO:0000269|PubMed:20346719}.
CC -!- SUBUNIT: Each stator complex is composed of 4 MotA and 2 MotB subunits;
CC in E.coli 11 to 12 stator complexes can be involved in flagellar
CC rotation. 2 A subunits and 1 B subunit are thought to form a single ion
CC channel, so that each stator complex contains two channels.
CC -!- INTERACTION:
CC P0AF06; P09348: motA; NbExp=2; IntAct=EBI-1117399, EBI-557926;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2447650};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:2447650}.
CC Note=The OmpA-like domain probably functions to anchor the complex to
CC the cell wall.
CC -!- SIMILARITY: Belongs to the MotB family. {ECO:0000305}.
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DR EMBL; J01652; AAA24178.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74959.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15710.1; -; Genomic_DNA.
DR EMBL; M34669; AAA23572.1; -; Genomic_DNA.
DR PIR; A64952; QRECMB.
DR RefSeq; NP_416403.1; NC_000913.3.
DR RefSeq; WP_000795630.1; NZ_STEB01000026.1.
DR AlphaFoldDB; P0AF06; -.
DR SMR; P0AF06; -.
DR BioGRID; 4261035; 417.
DR ComplexPortal; CPX-5884; Flagellar motor stator complex.
DR DIP; DIP-47996N; -.
DR IntAct; P0AF06; 5.
DR STRING; 511145.b1889; -.
DR TCDB; 1.A.30.1.1; the h(+)- or na(+)-translocating bacterial flagellar motor/exbbd outer membrane transport energizer (mot/exb) superfamily.
DR PaxDb; P0AF06; -.
DR PRIDE; P0AF06; -.
DR EnsemblBacteria; AAC74959; AAC74959; b1889.
DR EnsemblBacteria; BAA15710; BAA15710; BAA15710.
DR GeneID; 66674220; -.
DR GeneID; 946402; -.
DR KEGG; ecj:JW1878; -.
DR KEGG; eco:b1889; -.
DR PATRIC; fig|1411691.4.peg.358; -.
DR EchoBASE; EB0597; -.
DR eggNOG; COG1360; Bacteria.
DR HOGENOM; CLU_016890_3_0_6; -.
DR InParanoid; P0AF06; -.
DR OMA; DEKNRPM; -.
DR PhylomeDB; P0AF06; -.
DR BioCyc; EcoCyc:MOTB-FLAGELLAR-MOTOR-STATOR-PROTEIN; -.
DR PHI-base; PHI:6534; -.
DR PRO; PR:P0AF06; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009288; C:bacterial-type flagellum; IC:ComplexPortal.
DR GO; GO:0120101; C:bacterial-type flagellum stator complex; IPI:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoliWiki.
DR GO; GO:0015252; F:proton channel activity; TAS:EcoCyc.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IMP:EcoCyc.
DR GO; GO:0006935; P:chemotaxis; IC:ComplexPortal.
DR GO; GO:1902600; P:proton transmembrane transport; TAS:EcoCyc.
DR CDD; cd07185; OmpA_C-like; 1.
DR Gene3D; 3.30.1330.60; -; 1.
DR InterPro; IPR025713; MotB_N_dom.
DR InterPro; IPR006665; OmpA-like.
DR InterPro; IPR036737; OmpA-like_sf.
DR Pfam; PF13677; MotB_plug; 1.
DR Pfam; PF00691; OmpA; 1.
DR SUPFAM; SSF103088; SSF103088; 1.
DR PROSITE; PS51123; OMPA_2; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Chemotaxis; Flagellar rotation;
KW Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..308
FT /note="Motility protein B"
FT /id="PRO_0000189585"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:2447650"
FT TRANSMEM 28..49
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT TOPO_DOM 50..308
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:2447650"
FT DOMAIN 148..268
FT /note="OmpA-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00473"
FT REGION 73..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 31
FT /note="A->T: Complete loss of motility."
FT MUTAGEN 32
FT /note="D->N: Complete loss of motility."
FT /evidence="ECO:0000269|PubMed:2061285"
FT MUTAGEN 39
FT /note="A->V: Complete loss of motility."
FT /evidence="ECO:0000269|PubMed:2061285"
FT MUTAGEN 159
FT /note="P->I: Decreased motility, subnormal torque, tethered
FT strains rotate very slowly."
FT /evidence="ECO:0000269|PubMed:2061285"
FT MUTAGEN 164
FT /note="G->D: Complete loss of motility."
FT /evidence="ECO:0000269|PubMed:2061285"
FT MUTAGEN 196
FT /note="T->I: Complete loss of motility."
FT /evidence="ECO:0000269|PubMed:2061285"
FT MUTAGEN 197
FT /note="D->N: Complete loss of motility."
FT /evidence="ECO:0000269|PubMed:2061285"
FT MUTAGEN 205
FT /note="E->K: Decreased motility, subnormal torque, tethered
FT strains rotate very slowly, maybe reduced affinity for the
FT motor."
FT /evidence="ECO:0000269|PubMed:2061285"
FT MUTAGEN 214
FT /note="S->F: Complete loss of motility."
FT /evidence="ECO:0000269|PubMed:2061285"
FT MUTAGEN 217
FT /note="R->W: Complete loss of motility."
FT /evidence="ECO:0000269|PubMed:2061285"
FT MUTAGEN 222
FT /note="R->H: Complete loss of motility."
FT /evidence="ECO:0000269|PubMed:2061285"
FT MUTAGEN 240
FT /note="G->D: Decreased motility, subnormal torque, tethered
FT strains rotate very slowly."
FT /evidence="ECO:0000269|PubMed:2061285"
FT MUTAGEN 242
FT /note="A->T,V: Complete loss of motility."
FT /evidence="ECO:0000269|PubMed:2061285"
FT MUTAGEN 258
FT /note="R->C,H: Complete loss of motility."
FT /evidence="ECO:0000269|PubMed:2061285"
SQ SEQUENCE 308 AA; 34186 MW; 2F20C551C44BD6E3 CRC64;
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
