MOTA_AQUAE
ID MOTA_AQUAE Reviewed; 254 AA.
AC O67122;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Motility protein A;
DE AltName: Full=Chemotaxis protein MotA;
GN Name=motA; OrderedLocusNames=aq_1003;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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 membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MotA family. {ECO:0000305}.
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DR EMBL; AE000657; AAC07083.1; -; Genomic_DNA.
DR PIR; G70386; G70386.
DR RefSeq; NP_213685.1; NC_000918.1.
DR RefSeq; WP_010880623.1; NC_000918.1.
DR AlphaFoldDB; O67122; -.
DR SMR; O67122; -.
DR STRING; 224324.aq_1003; -.
DR EnsemblBacteria; AAC07083; AAC07083; aq_1003.
DR KEGG; aae:aq_1003; -.
DR PATRIC; fig|224324.8.peg.785; -.
DR eggNOG; COG1291; Bacteria.
DR HOGENOM; CLU_079895_1_0_0; -.
DR InParanoid; O67122; -.
DR OMA; EIETHHQ; -.
DR OrthoDB; 897037at2; -.
DR Proteomes; UP000000798; 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; IPR002898; MotA_ExbB_proton_chnl.
DR Pfam; PF01618; MotA_ExbB; 1.
DR PROSITE; PS01307; MOTA; 1.
PE 3: Inferred from homology;
KW Cell membrane; Chemotaxis; Flagellar rotation; Hydrogen ion transport;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..254
FT /note="Motility protein A"
FT /id="PRO_0000189569"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 254 AA; 27263 MW; 96308B6EE1A6213F CRC64;
MDVGTIIGII AAFLLILISI LIGGSITAFI NVPSIFIVVG GGMAAAMGAF PLKDFIRGVL
AIKKAFLWKP PDLNDVIETI GEIASKVRKE GILALEGDIE LYYQKDPLLG DMIRMLVDGI
DINDIKATAE MALAQLDEKM STEVAVWEKL ADLFPAFGMI GTLIGLIQML RNLNDPSALG
PGMAVALITT LYGAILANAF AIPVANKLKK AKDMEVLVKT IYIEAIEKIQ KGENPNVVKQ
EAAIMLGVEL PEEV