P96574 (MTLR_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcriptional regulator MtlR

Alternative name(s):
Mannitol operon transcriptional activator
Short name=Mtl operon transcriptional activator

Including the following 2 domains:

1. Putative phosphotransferase enzyme IIB component
   EC=2.7.1.69
   Alternative name(s):
   Putative PTS system EIIB component
2. Putative phosphotransferase enzyme IIA component
   EC=2.7.1.-
   Alternative name(s):
   Putative PTS system EIIA component

Gene names

Name:	mtlR
Synonyms:	ydaA
Ordered Locus Names:	BSU04160

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	694 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Positively regulates the expression of the mtlAFD operon involved in the uptake and catabolism of mannitol. Ref.3
Catalytic activity	Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate. Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine.
Induction	Up-regulated by mannitol or glucitol. Ref.3
Domain	The PTS EIIB type-2 domain may serve a regulatory function, through its phosphorylation activity. The PTS EIIA type-2 domain may serve a regulatory function, through its phosphorylation activity.
Disruption phenotype	Cells lacking this gene can not grow on either mannitol or glucitol as sole carbon source. Ref.3
Miscellaneous	Might be activated by phosphorylation of certain histidyl residues by HPr By similarity.
Sequence similarities	Belongs to the transcriptional antiterminator BglG family. Contains 2 PRD domains. Contains 1 PTS EIIA type-2 domain. Contains 1 PTS EIIB type-2 domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Domain	Repeat
Ligand	DNA-binding
Molecular function	Activator Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein-N(PI)-phosphohistidine-sugar phosphotransferase activity Inferred from electronic annotation. Source: EC sugar:hydrogen symporter 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 – 694	694	Transcriptional regulator MtlR		PRO_0000376081
Regions
	Domain	195 – 300	106	PRD 1
	Domain	305 – 410	106	PRD 2
	Domain	413 – 502	90	PTS EIIB type-2
	Domain	536 – 683	148	PTS EIIA type-2
Amino acid modifications
	Modified residue	230	1	Phosphohistidine Potential
	Modified residue	289	1	Phosphohistidine Potential
	Modified residue	342	1	Phosphohistidine Potential
	Modified residue	399	1	Phosphohistidine Potential
	Modified residue	419	1	Phosphocysteine; by EIIA By similarity
	Modified residue	599	1	Phosphohistidine; by HPr By similarity

Sequences

	Sequence		Length	Mass (Da)
	P96574 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 540D906A19318343	FASTA	694	78,853
	10 20 30 40 50 60 MYMTAREQKL LKHLLLQNRY ITVTELAELM QVSTRTIHRE LKSIKPLMET VGLTLDKQPG 70 80 90 100 110 120 KGLKAVGSPE GKQKLLTDLS YEQHEYSADE RKLLILCSLL ESQEPVKLYT LAHDLQVTNA 130 140 150 160 170 180 TVSYDLDELE KWISPFGLTL IRKRGFGIQL IGPENAKRKI VGNLIVNRLD IQMFLEAVEL 190 200 210 220 230 240 NIKGKTDSSE KMFGVVSKGE LLKMERILFQ LKEKIAFSLS DSSYIALVVH LTYAIERIKL 250 260 270 280 290 300 GETITMEQNE LEELMNAKEY SSALEIAGEL ERAFGVTIPE AEVGYITIHL RSANRKYKTE 310 320 330 340 350 360 YKAQEIELET ALQTKRLIAF ISDKIRMDLT KNYSLYEGLI AHLEPAVSRI KENIEIYNPM 370 380 390 400 410 420 KEQIKRDYFL LYMAIEEGVE KYFPGMSFSD DEIAFIVLHF GSALEIKKEE AKVKALVVCS 430 440 450 460 470 480 SGIGSSKMLA SRLKKELPEI ESFDMSSLIE LKGKDVQAYD MIVSTVPIPY ENIDYIMVSP 490 500 510 520 530 540 LLNEEDANQV KQYIKRKIPL ILNKKRSSKE EAQQADVPDM LEAAESIGRY MEVIQDVLRH 550 560 570 580 590 600 FTLAQLKTNP DHSMLLLELF QQLKKDGLIR DPEKAAVCLA EREKQGGLGI PGTNMALYHL 610 620 630 640 650 660 KNDEIVLPFF KMFDLSTPYE VDGMDGNTLR MTRILVMMAP GSLSAEGSEI LSAISSAIIE 670 680 690 SGESMAGFQE EGGQELYQRL NRIFFTWMKE KNIL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus subtilis genome." Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N. Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases 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]	"Mannitol-1-phosphate dehydrogenase (MtlD) is required for mannitol and glucitol assimilation in Bacillus subtilis: possible cooperation of mtl and gut operons." Watanabe S., Hamano M., Kakeshita H., Bunai K., Tojo S., Yamaguchi H., Fujita Y., Wong S.-L., Yamane K. J. Bacteriol. 185:4816-4824(2003) [PubMed: 12897001] [Abstract] Cited for: FUNCTION, INDUCTION, DISRUPTION PHENOTYPE. Strain: 168.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB001488 Genomic DNA. Translation: BAA19254.1. AL009126 Genomic DNA. Translation: CAB12223.1.
PIR	A69768.
RefSeq	NP_388297.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P96574.
SMR	P96574. Positions 202-294, 309-405, 413-494.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000003812; EBBACP00000003812; EBBACG00000003804.
GeneID	938253.
GenomeReviews	Gene locus BSU04160 in contig AL009126_GR.
KEGG	bsu:BSU04160.
NMPDR	fig|224308.1.peg.416.
PATRIC	18972410. VBIBacSub10457_0433.
Organism-specific databases
GenoList	BSU04160. [Micado]
Phylogenomic databases
GeneTree	EBGT00070000032076.
HOGENOM	HBG727344.
OMA	GYIAMHF.
PhylomeDB	P96574.
ProtClustDB	CLSK873726.
Enzyme and pathway databases
BioCyc	BSUB:BSU04160-MONOMER.
Family and domain databases
InterPro	IPR013196. HTH_11. IPR007737. Mga. IPR011608. PRD. IPR016152. PTrfase/Anion_transptr. IPR002178. PTS_EIIA_2. IPR013011. PTS_EIIB_2. IPR003501. PTS_EIIB_2/3. IPR011991. WHTH_trsnscrt_rep_DNA-bd. [Graphical view]
Gene3D	G3DSA:1.10.1790.10. PRD. 2 hits. G3DSA:3.40.930.10. PTS_EIIA_2. 1 hit. G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 2 hits.
KO	K03483.
Pfam	PF08279. HTH_11. 1 hit. PF05043. Mga. 1 hit. PF00874. PRD. 2 hits. PF02302. PTS_IIB. 1 hit. [Graphical view]
SUPFAM	SSF63520. PRD. 2 hits. SSF55804. PTrfase/Anion_transptr. 1 hit.
PROSITE	PS00654. PRD_1. False negative. PS51372. PRD_2. 2 hits. PS51094. PTS_EIIA_TYPE_2. 1 hit. PS00372. PTS_EIIA_TYPE_2_HIS. False negative. PS51099. PTS_EIIB_TYPE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MTLR_BACSU

Accession

Primary (citable) accession number: P96574
Secondary accession number(s): Q797N1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 26, 2009
Last sequence update:	May 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