MOTA_CERSP
ID MOTA_CERSP Reviewed; 253 AA.
AC Q53174;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Motility protein A;
DE AltName: Full=Chemotaxis protein MotA;
GN Name=motA;
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WS8;
RX PubMed=8596445; DOI=10.1111/j.1365-2958.1995.mmi_17050961.x;
RA Shah D.S.H., Sockett R.E.;
RT "Analysis of the motA flagellar motor gene from Rhodobacter sphaeroides, a
RT bacterium with a unidirectional, stop-start flagellum.";
RL Mol. Microbiol. 17:961-969(1995).
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; X85986; CAA59974.1; -; Genomic_DNA.
DR PIR; S70170; S70170.
DR AlphaFoldDB; Q53174; -.
DR SMR; Q53174; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097588; P:archaeal or bacterial-type flagellum-dependent cell motility; IEA:UniProtKB-KW.
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; IPR002898; MotA_ExbB_proton_chnl.
DR Pfam; PF01618; MotA_ExbB; 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; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..253
FT /note="Motility protein A"
FT /id="PRO_0000189577"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 253 AA; 27195 MW; B35462AAE123FDCC CRC64;
MDIAAAIGLI GAIVMVVGSM IYAGGVAPFV DIPSLVIVVA GTAFIVLAMK PLPVFLGHFK
AMMKVFKPSR FDMNEVISTM VELSNLARKD GIMALEGKAV PDAFFEKGLQ LLVDGTDEAK
LVKQLKYEIK AMKARHEAYQ GAVKAWIDIG PAMGMVGTLI GLVLMLGNMS DPKSIGPAMA
VALLTTLYGA LMANVIFAPI LNKLEGYSAD EVTYRELVIE GLRGIARGES ARMIEDQMVC
ALDRKQQMKR KAA