ID   MOTA_SALTY              Reviewed;         295 AA.
AC   P55891;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Motility protein A;
DE   AltName: Full=Chemotaxis protein MotA;
GN   Name=motA; OrderedLocusNames=STM1923;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SJW1103;
RX   PubMed=9139919; DOI=10.1128/jb.179.9.2994-3003.1997;
RA   Togashi F., Yamaguchi S., Kihara M., Aizawa S., Macnab R.M.;
RT   "An extreme clockwise switch bias mutation in fliG of Salmonella
RT   typhimurium and its suppression by slow-motile mutations in motA and
RT   motB.";
RL   J. Bacteriol. 179:2994-3003(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10586519; DOI=10.1266/ggs.74.105;
RA   Yanagihara S., Iyoda S., Ohnishi K., Iino T., Kutsukake K.;
RT   "Structure and transcriptional control of the flagellar master operon of
RT   Salmonella typhimurium.";
RL   Genes Genet. Syst. 74:105-111(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Each stator complex is composed of 4 MotA and 2 MotB subunits.
CC       2 A subunits and 1 B subunit are thought to form a single ion channel,
CC       so that each stator complex contains two channels (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the MotA family. {ECO:0000305}.
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DR   EMBL; U81861; AAC45265.1; -; Genomic_DNA.
DR   EMBL; D43640; BAA85316.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20839.1; -; Genomic_DNA.
DR   RefSeq; NP_460880.1; NC_003197.2.
DR   RefSeq; WP_000906312.1; NC_003197.2.
DR   AlphaFoldDB; P55891; -.
DR   SMR; P55891; -.
DR   IntAct; P55891; 1.
DR   STRING; 99287.STM1923; -.
DR   TCDB; 1.A.30.1.7; the h(+)- or na(+)-translocating bacterial flagellar motor/exbbd outer membrane transport energizer (mot/exb) superfamily.
DR   PaxDb; P55891; -.
DR   EnsemblBacteria; AAL20839; AAL20839; STM1923.
DR   GeneID; 1253444; -.
DR   KEGG; stm:STM1923; -.
DR   PATRIC; fig|99287.12.peg.2040; -.
DR   HOGENOM; CLU_068213_0_0_6; -.
DR   OMA; EIETHHQ; -.
DR   PhylomeDB; P55891; -.
DR   BioCyc; SENT99287:STM1923-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IBA:GO_Central.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
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   3: Inferred from homology;
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_0000189573"
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"
SQ   SEQUENCE   295 AA;  32082 MW;  DFD13EE6938CC641 CRC64;
     MLILLGYLVV IGTVFGGYVM TGGHLGALYQ PAELVIIGGA GIGAFIVGNN GKAIKGTMKA
     IPLLFRRSKY TKSMYMDLLA LLYRLMAKSR QQGMFSLERD IENPKESEIF ASYPRILADA
     VMLDFIVDYL RLIISGNMNT FEIEALMDEE IETHESEAEV PANSLAMVGD SLPAFGIVAA
     VMGVVHALAS ADRPAAELGA LIAHAMVGTF LGILLAYGFI SPLATVLRQK SAETTKMMQC
     VKITLLSNLN GYAPPIAVEF GRKTLYSSER PSFIELEEHV RAVRNPNQQQ TTEEA