MOTA_TREPA
ID MOTA_TREPA Reviewed; 259 AA.
AC O07886;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Motility protein A;
DE AltName: Full=Chemotaxis protein MotA;
GN Name=motA; OrderedLocusNames=TP_0725;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(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 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; U28219; AAB61253.1; -; Genomic_DNA.
DR EMBL; AE000520; AAC65690.1; -; Genomic_DNA.
DR PIR; A71292; A71292.
DR RefSeq; WP_010882170.1; NC_021490.2.
DR AlphaFoldDB; O07886; -.
DR SMR; O07886; -.
DR IntAct; O07886; 2.
DR STRING; 243276.TPANIC_0725; -.
DR EnsemblBacteria; AAC65690; AAC65690; TP_0725.
DR GeneID; 57879249; -.
DR KEGG; tpa:TP_0725; -.
DR eggNOG; COG1291; Bacteria.
DR HOGENOM; CLU_079895_1_0_12; -.
DR OMA; EIETHHQ; -.
DR OrthoDB; 897037at2; -.
DR Proteomes; UP000000811; Chromosome.
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; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..259
FT /note="Motility protein A"
FT /id="PRO_0000189578"
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; 28645 MW; C14B10A4B6CFB516 CRC64;
MDIASFIGLF GGFAIIIFGA VLGGSARGLF HVPSLLITVG GSYLTLFLTY PLSYAVGVFR
VIARVFHAAD FHEREIVQRL YALAEKSRRT GLLALEEEIQ DFDDDFVRTG LRNVVDGVDG
DAIKALMESE LTHMEDRHNT WISLLNSWAA LAPGYGMLGT VMGLIGMLAT LEDKSSLGSN
MATALITTFY GSLVQNWFIT PVATKLQYQH DLEVKSKEMV IEGVLSIQAG DHPRVLAQRL
LTYLSPKMRK ELEMELIKD