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Protein
Submitted name:

Leucine-responsive regulatory protein

Gene

lrp

Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • amino acid binding Source: MTBBASE
  • DNA binding Source: MTBBASE
  • sequence-specific DNA binding Source: InterPro
  • transcription factor activity, sequence-specific DNA binding Source: InterPro

GO - Biological processi

  • protein homooligomerization Source: MTBBASE
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulationUniRule annotation

Keywords - Ligandi

DNA-bindingUniRule annotation

Enzyme and pathway databases

BioCyciMTBRV:RV3291C-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
Leucine-responsive regulatory proteinImported
Gene namesi
Name:lrpImported
Ordered Locus Names:MT3390Imported
OrganismiMycobacterium tuberculosis (strain CDC 1551 / Oshkosh)Imported
Taxonomic identifieri83331 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001020 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IVMX-ray2.50A/B1-150[»]
2QZ8X-ray2.16A/B/C/D5-150[»]
2VBWX-ray2.20A/B1-150[»]
2VBXX-ray2.75A/B1-150[»]
2VBYX-ray2.80A/B1-150[»]
2VBZX-ray2.80A/B1-150[»]
2VC0X-ray2.50A/B1-150[»]
2VC1X-ray2.75A/B1-150[»]
2W24X-ray2.50A/B1-150[»]
2W25X-ray2.15A/B1-150[»]
2W29X-ray4.10A/B/C/D1-150[»]
ProteinModelPortaliP96896.
SMRiP96896. Positions 4-150.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 6662HTH asnC-type DNA-bindingInterPro annotationAdd
BLAST

Sequence similaritiesi

Contains 3 HTH asnC-type DNA-binding domains.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000115327.
KOiK03719.
OrthoDBiEOG6F29D2.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.70.920. 1 hit.
InterProiIPR000485. AsnC-type_HTH_dom.
IPR011008. Dimeric_a/b-barrel.
IPR019888. Tscrpt_reg_AsnC-typ.
IPR019887. Tscrpt_reg_AsnC/Lrp_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01037. AsnC_trans_reg. 1 hit.
PF13404. HTH_AsnC-type. 1 hit.
[Graphical view]
PRINTSiPR00033. HTHASNC.
SMARTiSM00344. HTH_ASNC. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF54909. SSF54909. 1 hit.
PROSITEiPS50956. HTH_ASNC_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P96896-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEALDDIDR ILVRELAADG RATLSELATR AGLSVSAVQS RVRRLESRGV
60 70 80 90 100
VQGYSARINP EAVGHLLSAF VAITPLDPSQ PDDAPARLEH IEEVESCYSV
110 120 130 140 150
AGEESYVLLV RVASARALED LLQRIRTTAN VRTRSTIILN TFYSDRQHIP
Length:150
Mass (Da):16,511
Last modified:May 1, 1997 - v1
Checksum:iEE59E5ED33D88CCE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000516 Genomic DNA. Translation: AAK47733.1.
PIRiD70981.
RefSeqiWP_003417179.1. NZ_KK341227.1.

Genome annotation databases

EnsemblBacteriaiAAK47733; AAK47733; MT3390.
KEGGimtc:MT3390.
PATRICi18129206. VBIMycTub22151_3699.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000516 Genomic DNA. Translation: AAK47733.1.
PIRiD70981.
RefSeqiWP_003417179.1. NZ_KK341227.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IVMX-ray2.50A/B1-150[»]
2QZ8X-ray2.16A/B/C/D5-150[»]
2VBWX-ray2.20A/B1-150[»]
2VBXX-ray2.75A/B1-150[»]
2VBYX-ray2.80A/B1-150[»]
2VBZX-ray2.80A/B1-150[»]
2VC0X-ray2.50A/B1-150[»]
2VC1X-ray2.75A/B1-150[»]
2W24X-ray2.50A/B1-150[»]
2W25X-ray2.15A/B1-150[»]
2W29X-ray4.10A/B/C/D1-150[»]
ProteinModelPortaliP96896.
SMRiP96896. Positions 4-150.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK47733; AAK47733; MT3390.
KEGGimtc:MT3390.
PATRICi18129206. VBIMycTub22151_3699.

Phylogenomic databases

HOGENOMiHOG000115327.
KOiK03719.
OrthoDBiEOG6F29D2.

Enzyme and pathway databases

BioCyciMTBRV:RV3291C-MONOMER.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.70.920. 1 hit.
InterProiIPR000485. AsnC-type_HTH_dom.
IPR011008. Dimeric_a/b-barrel.
IPR019888. Tscrpt_reg_AsnC-typ.
IPR019887. Tscrpt_reg_AsnC/Lrp_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01037. AsnC_trans_reg. 1 hit.
PF13404. HTH_AsnC-type. 1 hit.
[Graphical view]
PRINTSiPR00033. HTHASNC.
SMARTiSM00344. HTH_ASNC. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF54909. SSF54909. 1 hit.
PROSITEiPS50956. HTH_ASNC_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CDC 1551 / OshkoshImported.
  2. "Mechanistic insights from the crystal structures of a feast/famine regulatory protein from Mycobacterium tuberculosis H37Rv."
    Shrivastava T., Ramachandran R.
    Nucleic Acids Res. 35:7324-7335(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
  3. "Crystal structure of Mycobacterium tuberculosis LrpA, a leucine-responsive global regulator associated with starvation response."
    Reddy M.C., Gokulan K., Jacobs W.R., Ioerger T.R., Sacchettini J.C.
    Protein Sci. 17:159-170(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 5-150.
  4. "Ligand-induced structural transitions, mutational analysis, and 'open' quaternary structure of the M. tuberculosis feast/famine regulatory protein (Rv3291c)."
    Shrivastava T., Dey A., Ramachandran R.
    J. Mol. Biol. 392:1007-1019(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).

Entry informationi

Entry nameiP96896_MYCTO
AccessioniPrimary (citable) accession number: P96896
Secondary accession number(s): F2GKW4, Q7D5R8
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1997
Last sequence update: May 1, 1997
Last modified: May 11, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.