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Protein

Nitrogen regulation protein NR(I)

Gene

glnG

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Member of the two-component regulatory system NtrB/NtrC involved in the activation of nitrogen assimilatory genes such as GlnA. NtrC is phosphorylated by NtrB and interacts with sigma-54.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi168 – 1758ATPPROSITE-ProRule annotation
Nucleotide bindingi231 – 24010ATPPROSITE-ProRule annotation
DNA bindingi445 – 46420H-T-H motifBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Nitrogen fixation, Transcription, Transcription regulation, Two-component regulatory system

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciSENT99287:GCTI-4034-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrogen regulation protein NR(I)
Gene namesi
Name:glnG
Synonyms:ntrC
Ordered Locus Names:STM4005
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 469469Nitrogen regulation protein NR(I)PRO_0000081167Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 5414-aspartylphosphatePROSITE-ProRule annotation

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP41789.
PRIDEiP41789.

Interactioni

Protein-protein interaction databases

STRINGi99287.STM4005.

Structurei

Secondary structure

1
469
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93Combined sources
Beta strandi11 – 144Combined sources
Helixi15 – 239Combined sources
Turni24 – 274Combined sources
Beta strandi33 – 364Combined sources
Helixi38 – 425Combined sources
Beta strandi43 – 453Combined sources
Beta strandi51 – 533Combined sources
Beta strandi56 – 583Combined sources
Turni59 – 613Combined sources
Helixi66 – 727Combined sources
Beta strandi73 – 764Combined sources
Beta strandi78 – 814Combined sources
Turni88 – 903Combined sources
Beta strandi91 – 933Combined sources
Beta strandi98 – 1014Combined sources
Helixi108 – 12114Combined sources
Beta strandi390 – 3923Combined sources
Helixi402 – 41413Combined sources
Turni415 – 4173Combined sources
Helixi421 – 44020Combined sources
Turni441 – 4433Combined sources
Helixi447 – 4515Combined sources
Helixi456 – 46813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DC7NMR-A1-124[»]
1DC8NMR-A1-124[»]
1J56NMR-A1-124[»]
1KRWNMR-A1-124[»]
1KRXNMR-A1-124[»]
1NTCNMR-A/B380-469[»]
1NTRNMR-A1-124[»]
ProteinModelPortaliP41789.
SMRiP41789. Positions 1-124, 380-469.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41789.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 119115Response regulatoryPROSITE-ProRule annotationAdd
BLAST
Domaini140 – 369230Sigma-54 factor interactionPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 response regulatory domain.PROSITE-ProRule annotation
Contains 1 sigma-54 factor interaction domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105C1W. Bacteria.
COG2204. LUCA.
HOGENOMiHOG000058489.
KOiK07712.
OMAiGHSPVQV.
OrthoDBiEOG6WHNMG.
PhylomeDBiP41789.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR011006. CheY-like_superfamily.
IPR009057. Homeodomain-like.
IPR002197. HTH_Fis.
IPR027417. P-loop_NTPase.
IPR010114. Sig_transdc_resp-reg_NtrC.
IPR001789. Sig_transdc_resp-reg_receiver.
IPR002078. Sigma_54_int.
IPR025662. Sigma_54_int_dom_ATP-bd_1.
IPR025943. Sigma_54_int_dom_ATP-bd_2.
IPR025944. Sigma_54_int_dom_CS.
[Graphical view]
PfamiPF02954. HTH_8. 1 hit.
PF00072. Response_reg. 1 hit.
PF00158. Sigma54_activat. 1 hit.
[Graphical view]
PRINTSiPR01590. HTHFIS.
SMARTiSM00382. AAA. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF52172. SSF52172. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01818. ntrC. 1 hit.
PROSITEiPS50110. RESPONSE_REGULATORY. 1 hit.
PS00675. SIGMA54_INTERACT_1. 1 hit.
PS00676. SIGMA54_INTERACT_2. 1 hit.
PS00688. SIGMA54_INTERACT_3. 1 hit.
PS50045. SIGMA54_INTERACT_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41789-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRGIVWVVD DDSSIRWVLE RALAGAGLTC TTFENGNEVL AALASKTPDV
60 70 80 90 100
LLSDIRMPGM DGLALLKQIK QRHPMLPVII MTAHSDLDAA VSAYQQGAFD
110 120 130 140 150
YLPKPFDIDE AVALVERAIS HYQEQQQPRN IEVNGPTTDM IGEAPAMQDV
160 170 180 190 200
FRIIGRLSRS SISVLINGES GTGKELVAHA LHRHSPRAKA PFIALNMAAI
210 220 230 240 250
PKDLIESELF GHEKGAFTGA NTIRQGRFEQ ADGGTLFLDE IGDMPLDVQT
260 270 280 290 300
RLLRVLADGQ FYRVGGYAPV KVDVRIIAAT HQNLERRVQE GKFREDLFHR
310 320 330 340 350
LNVIRIHLPP LRERREDIPR LARHFLQVAA RELGVEAKLL HPETETALTR
360 370 380 390 400
LAWPGNVRQL ENTCRWLTVM AAGQEVLIQD LPGELFEAST PDSPSHLPPD
410 420 430 440 450
SWATLLAQWA DRALRSGHQN LLSEAQPELE RTLLTTALRH TQGHKQEAAR
460
LLGWGRNTLT RKLKELGME
Length:469
Mass (Da):52,271
Last modified:January 23, 2002 - v2
Checksum:i25D3100A2D707E05
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501V → L in CAA59425 (PubMed:7602583).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85104 Genomic DNA. Translation: CAA59425.1.
AE006468 Genomic DNA. Translation: AAL22844.1.
PIRiS53024.
RefSeqiNP_462885.1. NC_003197.1.
WP_001188783.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL22844; AAL22844; STM4005.
GeneIDi1255531.
KEGGistm:STM4005.
PATRICi32386882. VBISalEnt20916_4221.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85104 Genomic DNA. Translation: CAA59425.1.
AE006468 Genomic DNA. Translation: AAL22844.1.
PIRiS53024.
RefSeqiNP_462885.1. NC_003197.1.
WP_001188783.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DC7NMR-A1-124[»]
1DC8NMR-A1-124[»]
1J56NMR-A1-124[»]
1KRWNMR-A1-124[»]
1KRXNMR-A1-124[»]
1NTCNMR-A/B380-469[»]
1NTRNMR-A1-124[»]
ProteinModelPortaliP41789.
SMRiP41789. Positions 1-124, 380-469.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM4005.

Proteomic databases

PaxDbiP41789.
PRIDEiP41789.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL22844; AAL22844; STM4005.
GeneIDi1255531.
KEGGistm:STM4005.
PATRICi32386882. VBISalEnt20916_4221.

Phylogenomic databases

eggNOGiENOG4105C1W. Bacteria.
COG2204. LUCA.
HOGENOMiHOG000058489.
KOiK07712.
OMAiGHSPVQV.
OrthoDBiEOG6WHNMG.
PhylomeDBiP41789.

Enzyme and pathway databases

BioCyciSENT99287:GCTI-4034-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP41789.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR011006. CheY-like_superfamily.
IPR009057. Homeodomain-like.
IPR002197. HTH_Fis.
IPR027417. P-loop_NTPase.
IPR010114. Sig_transdc_resp-reg_NtrC.
IPR001789. Sig_transdc_resp-reg_receiver.
IPR002078. Sigma_54_int.
IPR025662. Sigma_54_int_dom_ATP-bd_1.
IPR025943. Sigma_54_int_dom_ATP-bd_2.
IPR025944. Sigma_54_int_dom_CS.
[Graphical view]
PfamiPF02954. HTH_8. 1 hit.
PF00072. Response_reg. 1 hit.
PF00158. Sigma54_activat. 1 hit.
[Graphical view]
PRINTSiPR01590. HTHFIS.
SMARTiSM00382. AAA. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF52172. SSF52172. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01818. ntrC. 1 hit.
PROSITEiPS50110. RESPONSE_REGULATORY. 1 hit.
PS00675. SIGMA54_INTERACT_1. 1 hit.
PS00676. SIGMA54_INTERACT_2. 1 hit.
PS00688. SIGMA54_INTERACT_3. 1 hit.
PS50045. SIGMA54_INTERACT_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Constitutive forms of the enhancer-binding protein NtrC: evidence that essential oligomerization determinants lie in the central activation domain."
    Flashner Y., Weiss D.S., Keener J., Kustu S.G.
    J. Mol. Biol. 249:700-713(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: LT2.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  3. "Three-dimensional solution structure of the N-terminal receiver domain of NTRC."
    Volkman B.F., Nohaile M.J., Amy N.K., Kustu S., Wemmer D.E.
    Biochemistry 34:1413-1424(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-124.
  4. "Solution structure of the DNA-binding domain of NtrC with three alanine substitutions."
    Pelton J.G., Kustu S., Wemmer D.E.
    J. Mol. Biol. 292:1095-1110(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 379-469.
  5. "Structure of a transiently phosphorylated switch in bacterial signal transduction."
    Kern D., Volkman B.F., Luginbuhl P., Nohaile M.J., Kustu S., Wemmer D.E.
    Nature 402:894-898(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-124.

Entry informationi

Entry nameiNTRC_SALTY
AccessioniPrimary (citable) accession number: P41789
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2002
Last modified: November 11, 2015
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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.