MOTA_ECOLI
ID MOTA_ECOLI Reviewed; 295 AA.
AC P09348;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 165.
DE RecName: Full=Motility protein A;
DE AltName: Full=Chemotaxis protein MotA;
GN Name=motA; Synonyms=flaJ; OrderedLocusNames=b1890, JW1879;
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=6090403; DOI=10.1128/jb.159.3.991-999.1984;
RA Dean G.E., Macnab R.M., Stader J., Matsumura P., Burks C.;
RT "Gene sequence and predicted amino acid sequence of the motA protein, a
RT membrane-associated protein required for flagellar rotation in Escherichia
RT coli.";
RL J. Bacteriol. 159:991-999(1984).
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 286-295.
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 [6]
RP MUTAGENESIS, AND TOPOLOGY.
RX PubMed=1719217; DOI=10.1016/0022-2836(91)90943-z;
RA Blair D.F., Berg H.C.;
RT "Mutations in the MotA protein of Escherichia coli reveal domains critical
RT for proton conduction.";
RL J. Mol. Biol. 221:1433-1442(1991).
RN [7]
RP MUTAGENESIS, AND TOPOLOGY.
RX PubMed=7643400; DOI=10.1006/jmbi.1995.0431;
RA Zhou J., Fazzio R.T., Blair D.F.;
RT "Membrane topology of the MotA protein of Escherichia coli.";
RL J. Mol. Biol. 251:237-242(1995).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [9]
RP INTERACTION WITH YCGR, AND MUTAGENESIS OF GLY-93 AND SER-96.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=20303158; DOI=10.1016/j.cell.2010.01.018;
RA Boehm A., Kaiser M., Li H., Spangler C., Kasper C.A., Ackermann M.,
RA Kaever V., Sourjik V., Roth V., Jenal U.;
RT "Second messenger-mediated adjustment of bacterial swimming velocity.";
RL Cell 141:107-116(2010).
RN [10]
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 [11]
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 rotation of the flagellar motor. Probable
CC transmembrane proton channel. Overexpression of MotA, with or without
CC MotB, restores motility in a pdeH disruption, (a c-di-GMP
CC phosphodiesterase) suggesting there is an interaction (direct or
CC indirect) between the c-di-GMP-binding flagellar brake protein YcgR and
CC the flagellar stator. {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. Interacts
CC with FliG. Interacts with flagellar brake protein YcgR in the flagellar
CC basal bodies (PubMed:20303158). In another study (PubMed:20346719) YcgR
CC was not seen to interact with MotA, but instead with FliM and FliG,
CC also in the flagellar basal body. {ECO:0000269|PubMed:20303158,
CC ECO:0000269|PubMed:20346719}.
CC -!- INTERACTION:
CC P09348; P0AF06: motB; NbExp=2; IntAct=EBI-557926, EBI-1117399;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the MotA family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J01652; AAA24177.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74960.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15711.1; -; Genomic_DNA.
DR PIR; A30279; QRECMA.
DR RefSeq; NP_416404.1; NC_000913.3.
DR RefSeq; WP_000906340.1; NZ_STEB01000026.1.
DR AlphaFoldDB; P09348; -.
DR SMR; P09348; -.
DR BioGRID; 4262245; 486.
DR ComplexPortal; CPX-5884; Flagellar motor stator complex.
DR DIP; DIP-10244N; -.
DR IntAct; P09348; 3.
DR STRING; 511145.b1890; -.
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; P09348; -.
DR PRIDE; P09348; -.
DR EnsemblBacteria; AAC74960; AAC74960; b1890.
DR EnsemblBacteria; BAA15711; BAA15711; BAA15711.
DR GeneID; 947564; -.
DR KEGG; ecj:JW1879; -.
DR KEGG; eco:b1890; -.
DR PATRIC; fig|1411691.4.peg.357; -.
DR EchoBASE; EB0596; -.
DR eggNOG; COG1291; Bacteria.
DR HOGENOM; CLU_068213_0_0_6; -.
DR InParanoid; P09348; -.
DR OMA; EIETHHQ; -.
DR PhylomeDB; P09348; -.
DR BioCyc; EcoCyc:MOTA-FLAGELLAR-MOTOR-STATOR-PROTEIN; -.
DR PHI-base; PHI:6533; -.
DR PRO; PR:P09348; -.
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:EcoCyc.
DR GO; GO:0015252; F:proton channel activity; TAS:EcoCyc.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IMP:EcoliWiki.
DR GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IC:ComplexPortal.
DR GO; GO:1902600; P:proton transmembrane transport; TAS:EcoCyc.
DR InterPro; IPR000540; Flag_MotA_CS.
DR InterPro; IPR022522; Flagellar_motor_stator_MotA.
DR InterPro; IPR002898; MotA_ExbB_proton_chnl.
DR PANTHER; PTHR30433:SF4; PTHR30433:SF4; 1.
DR Pfam; PF01618; MotA_ExbB; 1.
DR TIGRFAMs; TIGR03818; MotA1; 1.
DR PROSITE; PS01307; MOTA; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Chemotaxis; Flagellar rotation;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..295
FT /note="Motility protein A"
FT /id="PRO_0000189572"
FT TRANSMEM 2..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 22..33
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..200
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 93
FT /note="G->E: Suppresses pdeH disruption motility mutant,
FT swimming velocity is wild-type."
FT /evidence="ECO:0000269|PubMed:20303158"
FT MUTAGEN 93
FT /note="G->R: Suppresses pdeH disruption motility mutant,
FT swimming velocity is between disruption and wild-type."
FT /evidence="ECO:0000269|PubMed:20303158"
FT MUTAGEN 93
FT /note="G->V: Suppresses pdeH disruption motility mutant,
FT swimming velocity is between disruption and wild-type. In
FT the wt background velocity is reduced."
FT /evidence="ECO:0000269|PubMed:20303158"
FT MUTAGEN 96
FT /note="S->L: Suppresses pdeH disruption motility mutant,
FT swimming velocity is between disruption and wild-type. In
FT the wt background velocity is reduced."
FT /evidence="ECO:0000269|PubMed:20303158"
SQ SEQUENCE 295 AA; 32011 MW; 355DC13EF63DD7D8 CRC64;
MLILLGYLVV LGTVFGGYLM TGGSLGALYQ PAELVIIAGA GIGSFIVGNN GKAIKGTLKA
LPLLFRRSKY TKAMYMDLLA LLYRLMAKSR QMGMFSLERD IENPRESEIF ASYPRILADS
VMLDFIVDYL RLIISGHMNT FEIEALMDEE IETHESEAEV PANSLALVGD SLPAFGIVAA
VMGVVHALGS ADRPAAELGA LIAHAMVGTF LGILLAYGFI SPLATVLRQK SAETSKMMQC
VKVTLLSNLN GYAPPIAVEF GRKTLYSSER PSFIELEEHV RAVKNPQQQT TTEEA
