P71039 (MTA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
HTH-type transcriptional activator mta

Alternative name(s):
Multidrug transporter activation protein

Gene names

Name:	mta
Synonyms:	ywnD
Ordered Locus Names:	BSU36600

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	257 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Global transcriptional regulator that activates transcription of bmr and blt by binding directly to their promoter. Stimulates also the expression of the mta gene itself, ydfK and ymfE. Ref.3 Ref.4
Subunit structure	Homodimer. Ref.5 Ref.6
Subcellular location	Cytoplasm Probable.
Induction	Autoregulated. Ref.3
Domain	The central dimerization domain of the first subunit forms a two-helix antiparallel coiled coil with the dimerization domain of the second subunit.
Sequence similarities	Contains 1 HTH merR-type DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm
Domain	Coiled coil
Ligand	DNA-binding
Molecular function	Activator
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 257

257

HTH-type transcriptional activator mta

PRO_0000354974

Regions

Domain

2 – 71

70

HTH merR-type

DNA binding

5 – 24

20

H-T-H motif Ref.3

Region

71 – 74

4

Hinge

Region

76 – 104

29

Essential for dimerization

Coiled coil

76 – 107

32

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

257

Helix Strand Turn

Details...

Helix

5 – 11

7

Helix

16 – 24

9

Beta strand

31 – 33

3

Beta strand

39 – 41

3

Helix

43 – 57

15

Helix

62 – 70

9

Helix

76 – 105

30

Sequences

	Sequence		Length	Mass (Da)
	P71039 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 98AD46A5CED91DB0	FASTA	257	29,936
	10 20 30 40 50 60 MKYQVKQVAE ISGVSIRTLH HYDNIELLNP SALTDAGYRL YSDADLERLQ QILFFKEIGF 70 80 90 100 110 120 RLDEIKEMLD HPNFDRKAAL QSQKEILMKK KQRMDEMIQT IDRTLLSVDG GETMNKRDLF 130 140 150 160 170 180 AGLSMKDIEE HQQTYADEVR KLYGKEIAEE TEKRTSAYSA DDWRTIMAEF DSIYRRIAAR 190 200 210 220 230 240 MKHGPDDAEI QAAVGAFRDH ICQYHYDCTL DIFRGLGEVY ITDERFTDSI NQYGEGLAAF 250 LREAIIIYCD HQENPRP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Bacillus subtilis ureABC operon." Cruz-Ramos H., Glaser P., Wray L.V. Jr., Fisher S.H. J. Bacteriol. 179:3371-3373(1997) [PubMed: 9150240] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Mta, a global MerR-type regulator of the Bacillus subtilis multidrug-efflux transporters." Baranova N.N., Danchin A., Neyfakh A.A. Mol. Microbiol. 31:1549-1559(1999) [PubMed: 10200972] [Abstract] Cited for: FUNCTION, DNA-BINDING, INDUCTION. Strain: 168 / BD170.
[4]	"The major facilitator superfamily-type transporter YmfE and the multidrug-efflux activator Mta mediate bacillibactin secretion in Bacillus subtilis." Miethke M., Schmidt S., Marahiel M.A. J. Bacteriol. 190:5143-5152(2008) [PubMed: 18502870] [Abstract] Cited for: FUNCTION AS A REGULATOR OF YMFE. Strain: ATCC 21332 / IAM 1213.
[5]	"Crystal structure of MtaN, a global multidrug transporter gene activator." Godsey M.H., Baranova N.N., Neyfakh A.A., Brennan R.G. J. Biol. Chem. 276:47178-47184(2001) [PubMed: 11581256] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-109, SUBUNIT.
[6]	"The structural mechanism for transcription activation by MerR family member multidrug transporter activation, N terminus." Newberry K.J., Brennan R.G. J. Biol. Chem. 279:20356-20362(2004) [PubMed: 14985361] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-109 IN COMPLEX WITH DNA, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y08559 Genomic DNA. Translation: CAA69863.1.
AL009126 Genomic DNA. Translation: CAB15677.1.

PIR

C69661.

RefSeq

NP_391541.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JBG	X-ray	2.75	A	1-109	[»]
1R8D	X-ray	2.70	A/B	1-109	[»]

ProteinModelPortal

P71039.

SMR

P71039. Positions 1-144, 163-254.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000000479; EBBACP00000000479; EBBACG00000000477.

GeneID

936962.

GenomeReviews

Gene locus BSU36600 in contig AL009126_GR.

KEGG

bsu:BSU36600.

NMPDR

fig|224308.1.peg.3667.

PATRIC

18979348. VBIBacSub10457_3836.

Organism-specific databases

GenoList

BSU36600. [Micado]

Phylogenomic databases

GeneTree

EBGT00050000001456.

HOGENOM

HBG700494.

OMA

AKSENGY.

PhylomeDB

P71039.

ProtClustDB

CLSK2752536.

Enzyme and pathway databases

BioCyc

BSUB:BSU36600-MONOMER.

Family and domain databases

InterPro

IPR009061. DNA-bd_dom_put.
IPR012925. TipAS_dom.
IPR000551. Tscrpt_reg_HTH_MerR.
IPR015358. Tscrpt_reg_MerR_DNA-bd.
[Graphical view]

Pfam

PF00376. MerR. 1 hit.
PF09278. MerR-DNA-bind. 1 hit.
PF07739. TipAS. 1 hit.
[Graphical view]

PRINTS

PR00040. HTHMERR.

SMART

SM00422. HTH_MERR. 1 hit.
[Graphical view]

SUPFAM

SSF46955. Putativ_DNA_bind. 1 hit.

PROSITE

PS00552. HTH_MERR_1. False negative.
PS50937. HTH_MERR_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MTA_BACSU

Accession

Primary (citable) accession number: P71039
Secondary accession number(s): Q794Z9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	February 1, 1997
Last modified:	January 25, 2012
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program