P19466 (MTRB_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription attenuation protein MtrB

Alternative name(s):
Trp RNA-binding attenuation protein
Short name=TRAP
Tryptophan RNA-binding attenuator protein

Gene names

Name:	mtrB
Ordered Locus Names:	BSU22770

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	75 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for transcription attenuation control in the Trp operon. This trans-acting factor seems to recognize a 10 bases nucleotide sequence in the Trp leader transcript causing transcription termination. Binds the leader RNA only in presence of L-tryptophan. Ref.3
Subunit structure	Oligomer of 11 identical subunits arranged in doughnut-like structure.
Sequence similarities	Belongs to the MtrB family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Ligand	RNA-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA-dependent transcription, termination Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	RNA binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 75

75

Transcription attenuation protein MtrB HAMAP-Rule MF_00798

PRO_0000206028

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

75

Helix Strand Turn

Details...

Beta strand

9 – 16

8

Beta strand

19 – 25

7

Beta strand

27 – 29

3

Beta strand

32 – 38

7

Beta strand

43 – 47

5

Beta strand

50 – 65

16

Beta strand

68 – 70

3

Sequences

	Sequence		Length	Mass (Da)
	P19466 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 34C173A8D15A4B31	FASTA	75	8,328
	10 20 30 40 50 60 MNQKHSSDFV VIKAVEDGVN VIGLTRGTDT KFHHSEKLDK GEVIIAQFTE HTSAIKVRGE 70 ALIQTAYGEM KSEKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The mtr locus is a two-gene operon required for transcription attenuation in the trp operon of Bacillus subtilis." Gollnick P., Ishino S., Kuroda M.I., Henner D.J., Yanofsky C. Proc. Natl. Acad. Sci. U.S.A. 87:8726-8730(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA), an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of tryptophan biosynthesis." Babitzke P., Gollnick P., Yanofsky C. J. Bacteriol. 174:2059-2064(1992) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[4]	"The structure of trp RNA-binding attenuation protein." Antson A.A., Otridge J., Brzozowski A.M., Dodson E.J., Dodson G.G., Wilson K.S., Smith T.M., Yan M., Kurecki T., Gollnick P. Nature 374:693-700(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[5]	"11-fold symmetry of the trp RNA-binding attenuation protein (TRAP) from Bacillus subtilis determined by X-ray analysis." Antson A.A., Brzozowski A.M., Dodson E.J., Dauter Z., Wilson K.S., Kurecki T., Otridge J., Gollnick P. J. Mol. Biol. 244:1-5(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M37320 Genomic DNA. Translation: AAA22616.1.
M80245 Genomic DNA. Translation: AAA20853.1.
AL009126 Genomic DNA. Translation: CAB14193.1.

PIR

B38256.

RefSeq

NP_390158.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WAP	X-ray	1.80	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V	1-75	[»]
3ZZQ	X-ray	1.75	A/B/C/D/E/F	7-71	[»]
4B27	X-ray	2.72	A/B/C/D/E/F	1-75	[»]

ProteinModelPortal

P19466.

SMR

P19466. Positions 8-75.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU22770.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB14193; CAB14193; BSU22770.

GeneID

938996.

KEGG

bsu:BSU22770.

PATRIC

18976365. VBIBacSub10457_2373.

Organism-specific databases

GenoList

BSU22770. [Micado]

Phylogenomic databases

HOGENOM

HOG000245485.

KO

K06285.

OMA

FHHTEKL.

ProtClustDB

PRK13251.

Enzyme and pathway databases

BioCyc

BSUB:BSU22770-MONOMER.

Family and domain databases

Gene3D

2.60.40.50. 1 hit.

HAMAP

MF_00798. Trp_attenuator.

InterPro

IPR000824. Trp_RNA-bd_attenuator.
IPR016031. Trp_RNA-bd_attenuator-like_dom.
IPR023558. Trp_RNA-bd_attenuator_dom.
[Graphical view]

Pfam

PF02081. TrpBP. 1 hit.
[Graphical view]

PRINTS

PR00687. TRPRNAAP.

SUPFAM

SSF51219. TrpBP. 1 hit.

ProtoNet

Search...

Other

DrugBank

DB00150. L-Tryptophan.

EvolutionaryTrace

P19466.

Entry information

Entry name

MTRB_BACSU

Accession

Primary (citable) accession number: P19466

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	May 1, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program