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MOTA_BACSU
ID   MOTA_BACSU              Reviewed;         270 AA.
AC   P28611;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Motility protein A;
DE   AltName: Full=Chemotaxis protein MotA;
GN   Name=motA; OrderedLocusNames=BSU13690;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1624413; DOI=10.1128/jb.174.13.4197-4204.1992;
RA   Mirel D.B., Lustre V.M., Chamberlin M.J.;
RT   "An operon of Bacillus subtilis motility genes transcribed by the sigma D
RT   form of RNA polymerase.";
RL   J. Bacteriol. 174:4197-4204(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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; M77238; AAA22602.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13242.1; -; Genomic_DNA.
DR   PIR; A42882; A42882.
DR   RefSeq; NP_389252.1; NC_000964.3.
DR   RefSeq; WP_003244739.1; NZ_JNCM01000035.1.
DR   PDB; 6YSL; EM; 3.50 A; C/D/E/F/G=1-270.
DR   PDBsum; 6YSL; -.
DR   AlphaFoldDB; P28611; -.
DR   SMR; P28611; -.
DR   IntAct; P28611; 1.
DR   STRING; 224308.BSU13690; -.
DR   TCDB; 1.A.30.1.3; the h(+)- or na(+)-translocating bacterial flagellar motor/exbbd outer membrane transport energizer (mot/exb) superfamily.
DR   jPOST; P28611; -.
DR   PaxDb; P28611; -.
DR   PRIDE; P28611; -.
DR   EnsemblBacteria; CAB13242; CAB13242; BSU_13690.
DR   GeneID; 939302; -.
DR   KEGG; bsu:BSU13690; -.
DR   PATRIC; fig|224308.179.peg.1486; -.
DR   eggNOG; COG1291; Bacteria.
DR   InParanoid; P28611; -.
DR   OMA; EIETHHQ; -.
DR   PhylomeDB; P28611; -.
DR   BioCyc; BSUB:BSU13690-MON; -.
DR   Proteomes; UP000001570; 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   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Chemotaxis; Flagellar rotation;
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..270
FT                   /note="Motility protein A"
FT                   /id="PRO_0000189570"
FT   TRANSMEM        4..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        182..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        204..270
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   HELIX           4..23
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   TURN            29..31
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   TURN            36..39
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   HELIX           40..50
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   STRAND          55..58
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   HELIX           59..63
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   HELIX           75..78
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   TURN            79..81
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   STRAND          82..84
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   HELIX           85..92
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   TURN            98..101
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   HELIX           107..116
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   HELIX           123..169
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   STRAND          170..172
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   STRAND          175..177
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   HELIX           178..198
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   HELIX           201..231
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   TURN            235..237
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   HELIX           239..242
FT                   /evidence="ECO:0007829|PDB:6YSL"
FT   HELIX           248..251
FT                   /evidence="ECO:0007829|PDB:6YSL"
SQ   SEQUENCE   270 AA;  29339 MW;  81CF32526BB43C41 CRC64;
     MDKTSLIGII LAFVALSVGM VLKGVSFSAL ANPAAILIII AGTISAVVIA FPTKEIKKVP
     TLFRVLFKEN KQLTIEELIP MFSEWAQLAR REGLLALEAS IEDVDDAFLK NGLSMAVDGQ
     SAEFIRDIMT EEVEAMEDRH QAGAAIFTQA GTYAPTLGVL GAVIGLIAAL SHMDNTDELG
     HAISAAFVAT LLGIFTGYVL WHPFANKLKR KSKQEVKLRE VMIEGVLSVL EGQAPKVIEQ
     KLLMYLPAKD RLKFAEQGEA QNGEKKEEEA
 
 
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