MTA_BACSU
ID MTA_BACSU Reviewed; 257 AA.
AC P71039; Q794Z9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=HTH-type transcriptional activator mta;
DE AltName: Full=Multidrug transporter activation protein;
GN Name=mta; Synonyms=ywnD; OrderedLocusNames=BSU36600;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9150240; DOI=10.1128/jb.179.10.3371-3373.1997;
RA Cruz-Ramos H., Glaser P., Wray L.V. Jr., Fisher S.H.;
RT "The Bacillus subtilis ureABC operon.";
RL J. Bacteriol. 179:3371-3373(1997).
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).
RN [3]
RP FUNCTION, DNA-BINDING, AND INDUCTION.
RC STRAIN=168 / BD170;
RX PubMed=10200972; DOI=10.1046/j.1365-2958.1999.01301.x;
RA Baranova N.N., Danchin A., Neyfakh A.A.;
RT "Mta, a global MerR-type regulator of the Bacillus subtilis multidrug-
RT efflux transporters.";
RL Mol. Microbiol. 31:1549-1559(1999).
RN [4]
RP FUNCTION AS A REGULATOR OF YMFE.
RC STRAIN=ATCC 21332 / IAM 1213;
RX PubMed=18502870; DOI=10.1128/jb.00464-08;
RA Miethke M., Schmidt S., Marahiel M.A.;
RT "The major facilitator superfamily-type transporter YmfE and the multidrug-
RT efflux activator Mta mediate bacillibactin secretion in Bacillus
RT subtilis.";
RL J. Bacteriol. 190:5143-5152(2008).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-109, AND SUBUNIT.
RX PubMed=11581256; DOI=10.1074/jbc.m105819200;
RA Godsey M.H., Baranova N.N., Neyfakh A.A., Brennan R.G.;
RT "Crystal structure of MtaN, a global multidrug transporter gene
RT activator.";
RL J. Biol. Chem. 276:47178-47184(2001).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-109 IN COMPLEX WITH DNA, AND
RP SUBUNIT.
RX PubMed=14985361; DOI=10.1074/jbc.m400960200;
RA Newberry K.J., Brennan R.G.;
RT "The structural mechanism for transcription activation by MerR family
RT member multidrug transporter activation, N terminus.";
RL J. Biol. Chem. 279:20356-20362(2004).
CC -!- FUNCTION: Global transcriptional regulator that activates transcription
CC of bmr and blt by binding directly to their promoter. Stimulates also
CC the expression of the mta gene itself, ydfK and ymfE.
CC {ECO:0000269|PubMed:10200972, ECO:0000269|PubMed:18502870}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11581256,
CC ECO:0000269|PubMed:14985361}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Autoregulated. {ECO:0000269|PubMed:10200972}.
CC -!- DOMAIN: The central dimerization domain of the first subunit forms a
CC two-helix antiparallel coiled coil with the dimerization domain of the
CC second subunit.
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DR EMBL; Y08559; CAA69863.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15677.1; -; Genomic_DNA.
DR PIR; C69661; C69661.
DR RefSeq; NP_391541.1; NC_000964.3.
DR RefSeq; WP_003242936.1; NZ_JNCM01000034.1.
DR PDB; 1JBG; X-ray; 2.75 A; A=1-109.
DR PDB; 1R8D; X-ray; 2.70 A; A/B=1-109.
DR PDBsum; 1JBG; -.
DR PDBsum; 1R8D; -.
DR AlphaFoldDB; P71039; -.
DR SMR; P71039; -.
DR STRING; 224308.BSU36600; -.
DR PaxDb; P71039; -.
DR EnsemblBacteria; CAB15677; CAB15677; BSU_36600.
DR GeneID; 936962; -.
DR KEGG; bsu:BSU36600; -.
DR PATRIC; fig|224308.179.peg.3961; -.
DR eggNOG; COG0789; Bacteria.
DR InParanoid; P71039; -.
DR OMA; DGFDHTQ; -.
DR PhylomeDB; P71039; -.
DR BioCyc; BSUB:BSU36600-MON; -.
DR EvolutionaryTrace; P71039; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.490.50; -; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR000551; MerR-type_HTH_dom.
DR InterPro; IPR036244; TipA-like_antibiotic-bd.
DR InterPro; IPR012925; TipAS_dom.
DR Pfam; PF13411; MerR_1; 1.
DR Pfam; PF07739; TipAS; 1.
DR PRINTS; PR00040; HTHMERR.
DR SMART; SM00422; HTH_MERR; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
DR SUPFAM; SSF89082; SSF89082; 1.
DR PROSITE; PS50937; HTH_MERR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Coiled coil; Cytoplasm; DNA-binding;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..257
FT /note="HTH-type transcriptional activator mta"
FT /id="PRO_0000354974"
FT DOMAIN 2..71
FT /note="HTH merR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
FT DNA_BIND 5..24
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
FT REGION 71..74
FT /note="Hinge"
FT REGION 76..104
FT /note="Essential for dimerization"
FT COILED 76..107
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:1R8D"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:1R8D"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1R8D"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1R8D"
FT HELIX 43..57
FT /evidence="ECO:0007829|PDB:1R8D"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:1R8D"
FT HELIX 76..105
FT /evidence="ECO:0007829|PDB:1R8D"
SQ SEQUENCE 257 AA; 29936 MW; 98AD46A5CED91DB0 CRC64;
MKYQVKQVAE ISGVSIRTLH HYDNIELLNP SALTDAGYRL YSDADLERLQ QILFFKEIGF
RLDEIKEMLD HPNFDRKAAL QSQKEILMKK KQRMDEMIQT IDRTLLSVDG GETMNKRDLF
AGLSMKDIEE HQQTYADEVR KLYGKEIAEE TEKRTSAYSA DDWRTIMAEF DSIYRRIAAR
MKHGPDDAEI QAAVGAFRDH ICQYHYDCTL DIFRGLGEVY ITDERFTDSI NQYGEGLAAF
LREAIIIYCD HQENPRP
