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Database: UniProt
Entry: P71039
LinkDB: P71039
Original site: P71039 
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   02-JUN-2021, entry version 134.
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   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; WGDTDAW; -.
DR   PhylomeDB; P71039; -.
DR   BioCyc; BSUB:BSU36600-MONOMER; -.
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
//
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