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   24-JAN-2024, entry version 123.
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; Pseudomonadota; 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; 511145-b1889; -.
DR   EnsemblBacteria; AAC74959; AAC74959; b1889.
DR   GeneID; 75171962; -.
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   OrthoDB; 9809186at2; -.
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; NAS:ComplexPortal.
DR   GO; GO:0120101; C:bacterial-type flagellum stator complex; IPI:ComplexPortal.
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; NAS:ComplexPortal.
DR   GO; GO:1902600; P:proton transmembrane transport; TAS:EcoCyc.
DR   CDD; cd07185; OmpA_C-like; 1.
DR   Gene3D; 3.30.1330.60; OmpA-like domain; 1.
DR   InterPro; IPR025713; MotB-like_N_dom.
DR   InterPro; IPR006665; OmpA-like.
DR   InterPro; IPR036737; OmpA-like_sf.
DR   PANTHER; PTHR30329:SF18; MOTILITY PROTEIN B; 1.
DR   PANTHER; PTHR30329; STATOR ELEMENT OF FLAGELLAR MOTOR COMPLEX; 1.
DR   Pfam; PF13677; MotB_plug; 1.
DR   Pfam; PF00691; OmpA; 1.
DR   SUPFAM; SSF103088; OmpA-like; 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
//