ID   MOTA_TREPH              Reviewed;         259 AA.
AC   Q56331; Q56327;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Motility protein A;
DE   AltName: Full=Chemotaxis protein MotA;
GN   Name=motA;
OS   Treponema phagedenis.
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=162;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Kazan 5;
RX   PubMed=8755894; DOI=10.1128/jb.178.15.4628-4634.1996;
RA   Limberger R.J., Slivienski L.L., El-Afandi M.C.T., Dantuono L.A.;
RT   "Organization, transcription, and expression of the 5' region of the fla
RT   operon of Treponema phagedenis and Treponema pallidum.";
RL   J. Bacteriol. 178:4628-4634(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-159.
RC   STRAIN=Kazan 5;
RX   PubMed=8206841; DOI=10.1128/jb.176.12.3631-3637.1994;
RA   Limberger R.J., Slivienski L.L., Samsonoff W.A.;
RT   "Genetic and biochemical analysis of the flagellar hook of Treponema
RT   phagedenis.";
RL   J. Bacteriol. 176:3631-3637(1994).
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; U32475; AAB03250.1; -; Genomic_DNA.
DR   EMBL; U04619; AAA73468.1; -; Genomic_DNA.
DR   RefSeq; WP_002700959.1; NZ_AQCF01000036.1.
DR   AlphaFoldDB; Q56331; -.
DR   SMR; Q56331; -.
DR   GeneID; 57754520; -.
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..259
FT                   /note="Motility protein A"
FT                   /id="PRO_0000189579"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        205..259
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   259 AA;  28739 MW;  C172A032FE37C54C CRC64;
     MDLASFIGFF GAFAIILMGG ILGGSASGFF HLPSVFITVG GSYLTLFLAY PLSYTLGIFK
     VCARVFKSAD FHEKEIVQRL YALAEKSRRT GLLALEEEIQ DFDDEFMRTG LRNVVDGIDG
     EAIRNLMENE LSHMEERHNR WISFINAWAT LAPGYGMLGT VMGLIGMLMA LEDKSSLGQN
     MAVALVTTLY GSLMANWLLI PMATKLGLQH EAEVKSKEMI IEGVLAIQAG DHPRILAQRL
     LVYLNPKDKR ELEAELIKD