MOTB_BACSU
ID MOTB_BACSU Reviewed; 261 AA.
AC P28612;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Motility protein B;
DE AltName: Full=Chemotaxis protein MotB;
GN Name=motB; OrderedLocusNames=BSU13680;
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 the rotation of the flagellar motor. Might
CC be a linker that fastens the torque-generating machinery to the cell
CC wall (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}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MotB family. {ECO:0000305}.
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DR EMBL; M77238; AAA22603.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13241.1; -; Genomic_DNA.
DR PIR; B42882; B42882.
DR RefSeq; NP_389251.1; NC_000964.3.
DR RefSeq; WP_003232473.1; NZ_JNCM01000035.1.
DR PDB; 6YSL; EM; 3.50 A; A/B=1-261.
DR PDBsum; 6YSL; -.
DR AlphaFoldDB; P28612; -.
DR SMR; P28612; -.
DR IntAct; P28612; 1.
DR STRING; 224308.BSU13680; -.
DR TCDB; 1.A.30.1.3; the h(+)- or na(+)-translocating bacterial flagellar motor/exbbd outer membrane transport energizer (mot/exb) superfamily.
DR PaxDb; P28612; -.
DR PRIDE; P28612; -.
DR EnsemblBacteria; CAB13241; CAB13241; BSU_13680.
DR GeneID; 939304; -.
DR KEGG; bsu:BSU13680; -.
DR PATRIC; fig|224308.179.peg.1485; -.
DR eggNOG; COG1360; Bacteria.
DR InParanoid; P28612; -.
DR OMA; DEKNRPM; -.
DR PhylomeDB; P28612; -.
DR BioCyc; BSUB:BSU13680-MON; -.
DR Proteomes; UP000001570; 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 CDD; cd07185; OmpA_C-like; 1.
DR Gene3D; 3.30.1330.60; -; 1.
DR InterPro; IPR025713; MotB_N_dom.
DR InterPro; IPR006665; OmpA-like.
DR InterPro; IPR036737; OmpA-like_sf.
DR Pfam; PF13677; MotB_plug; 1.
DR Pfam; PF00691; OmpA; 1.
DR SUPFAM; SSF103088; SSF103088; 1.
DR PROSITE; PS51123; OMPA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Chemotaxis; Flagellar rotation; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..261
FT /note="Motility protein B"
FT /id="PRO_0000189584"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..261
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 132..254
FT /note="OmpA-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00473"
FT REGION 68..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 19..36
FT /evidence="ECO:0007829|PDB:6YSL"
SQ SEQUENCE 261 AA; 29483 MW; BED623BE2A84C6D5 CRC64;
MARKKKKKHE DEHVDESWLV PYADILTLLL ALFIVLYASS SIDAAKFQML SKSFNEVFTG
GTGVLDYSSV TPPENESDGI DEVKKEKEEK EKNKKEKEKA ADQEELENVK SQVEKFIKDK
KLEHQLETKM TSEGLLITIK DSIFFDSGKA TIRKEDVPLA KEISNLLVIN PPRNIIISGH
TDNMPIKNSE FQSNWHLSVM RAVNFMGLLI ENPKLDAKVF SAKGYGEYKP VASNKTAEGR
SKNRRVEVLI LPRGAAETNE K
