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Protein
Submitted name:

Transcriptional regulator (NtrC family)

Gene

ntrC1

Organism
Aquifex aeolicus (strain VF5)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei140 – 1401ATP; via amide nitrogen and carbonyl oxygenCombined sources
Binding sitei239 – 2391ADPCombined sources
Binding sitei280 – 2801ATPCombined sources
Binding sitei299 – 2991ATPCombined sources
Binding sitei357 – 3571ATPCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi137 – 1404ADPCombined sources
Nucleotide bindingi169 – 1757ADPCombined sources
Nucleotide bindingi169 – 1757ATPCombined sources
Nucleotide bindingi357 – 3604ADPCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulationUniRule annotationSAAS annotation

Keywords - Ligandi

ATP-bindingUniRule annotationCombined sourcesSAAS annotation, DNA-bindingSAAS annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciAAEO224324:GJBH-797-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
Transcriptional regulator (NtrC family)Imported
Gene namesi
Name:ntrC1Imported
Ordered Locus Names:aq_1117Imported
OrganismiAquifex aeolicus (strain VF5)Imported
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
Proteomesi
  • UP000000798 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi158 ↔ 161Combined sources

Interactioni

Protein-protein interaction databases

DIPiDIP-59014N.
STRINGi224324.aq_1117.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NY5X-ray2.40A/B1-387[»]
1NY6X-ray3.10A/B/C/D/E/F/G/H/I/J/K/L/M/N122-387[»]
1ZY2X-ray3.03A/B1-136[»]
3M0EX-ray2.63A/B/C/D/E/F/G122-387[»]
4BS1electron microscopy18.00A312-384[»]
B137-309[»]
4BT0electron microscopy17.00A312-384[»]
B137-309[»]
4BT1electron microscopy16.00A312-384[»]
B137-309[»]
4L4UX-ray2.20A1-439[»]
4L5EX-ray1.34A393-438[»]
4LY6X-ray3.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X121-387[»]
4LZZX-ray3.21A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X121-387[»]
ProteinModelPortaliO67198.
SMRiO67198. Positions 1-385.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO67198.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 116115Response regulatoryInterPro annotationAdd
BLAST
Domaini139 – 368230Sigma-54 factor interactionInterPro annotationAdd
BLAST

Sequence similaritiesi

Contains 1 sigma-54 factor interaction domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C1W. Bacteria.
COG2204. LUCA.
HOGENOMiHOG000058489.
InParanoidiO67198.
KOiK02481.
OMAiNNIITER.
OrthoDBiEOG6WHNMG.

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.
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.
[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.
PROSITEiPS50110. RESPONSE_REGULATORY. 1 hit.
PS00675. SIGMA54_INTERACT_1. 1 hit.
PS00676. SIGMA54_INTERACT_2. 1 hit.
PS50045. SIGMA54_INTERACT_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O67198-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVLVIEDDK VFRGLLEEYL SMKGIKVESA ERGKEAYKLL SEKHFNVVLL
60 70 80 90 100
DLLLPDVNGL EILKWIKERS PETEVIVITG HGTIKTAVEA MKMGAYDFLT
110 120 130 140 150
KPCMLEEIEL TINKAIEHRK LRKENELLRR EKDLKEEEYV FESPKMKEIL
160 170 180 190 200
EKIKKISCAE CPVLITGESG VGKEVVARLI HKLSDRSKEP FVALNVASIP
210 220 230 240 250
RDIFEAELFG YEKGAFTGAV SSKEGFFELA DGGTLFLDEI GELSLEAQAK
260 270 280 290 300
LLRVIESGKF YRLGGRKEIE VNVRILAATN RNIKELVKEG KFREDLYYRL
310 320 330 340 350
GVIEIEIPPL RERKEDIIPL ANHFLKKFSR KYAKEVEGFT KSAQELLLSY
360 370 380 390 400
PWYGNVRELK NVIERAVLFS EGKFIDRGEL SCLVNSKGIK NKHKSIKEIE
410 420 430
KEEIIKVLKE VNFNKKLASE ILGIPLRTLY RRLKEYGIE
Length:439
Mass (Da):50,367
Last modified:August 1, 1998 - v1
Checksum:iAAE1E9780271DFC0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC07159.1.
PIRiC70396.
RefSeqiNP_213762.1. NC_000918.1.
WP_010880700.1. NC_000918.1.

Genome annotation databases

EnsemblBacteriaiAAC07159; AAC07159; aq_1117.
GeneIDi1192544.
KEGGiaae:aq_1117.
PATRICi20959504. VBIAquAeo85532_0872.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC07159.1.
PIRiC70396.
RefSeqiNP_213762.1. NC_000918.1.
WP_010880700.1. NC_000918.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NY5X-ray2.40A/B1-387[»]
1NY6X-ray3.10A/B/C/D/E/F/G/H/I/J/K/L/M/N122-387[»]
1ZY2X-ray3.03A/B1-136[»]
3M0EX-ray2.63A/B/C/D/E/F/G122-387[»]
4BS1electron microscopy18.00A312-384[»]
B137-309[»]
4BT0electron microscopy17.00A312-384[»]
B137-309[»]
4BT1electron microscopy16.00A312-384[»]
B137-309[»]
4L4UX-ray2.20A1-439[»]
4L5EX-ray1.34A393-438[»]
4LY6X-ray3.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X121-387[»]
4LZZX-ray3.21A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X121-387[»]
ProteinModelPortaliO67198.
SMRiO67198. Positions 1-385.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59014N.
STRINGi224324.aq_1117.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC07159; AAC07159; aq_1117.
GeneIDi1192544.
KEGGiaae:aq_1117.
PATRICi20959504. VBIAquAeo85532_0872.

Phylogenomic databases

eggNOGiENOG4105C1W. Bacteria.
COG2204. LUCA.
HOGENOMiHOG000058489.
InParanoidiO67198.
KOiK02481.
OMAiNNIITER.
OrthoDBiEOG6WHNMG.

Enzyme and pathway databases

BioCyciAAEO224324:GJBH-797-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO67198.

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.
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.
[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.
PROSITEiPS50110. RESPONSE_REGULATORY. 1 hit.
PS00675. SIGMA54_INTERACT_1. 1 hit.
PS00676. SIGMA54_INTERACT_2. 1 hit.
PS50045. SIGMA54_INTERACT_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: VF5Imported.
  2. "Regulation of the transcriptional activator NtrC1: structural studies of the regulatory and AAA+ ATPase domains."
    Lee S.Y., De La Torre A., Yan D., Kustu S., Nixon B.T., Wemmer D.E.
    Genes Dev. 17:2552-2563(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-387 IN COMPLEX WITH ADP.
  3. "Negative regulation of AAA + ATPase assembly by two component receiver domains: a transcription activation mechanism that is conserved in mesophilic and extremely hyperthermophilic bacteria."
    Doucleff M., Chen B., Maris A.E., Wemmer D.E., Kondrashkina E., Nixon B.T.
    J. Mol. Biol. 353:242-255(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.03 ANGSTROMS) OF 1-136.
  4. "Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase."
    Chen B., Sysoeva T.A., Chowdhury S., Guo L., De Carlo S., Hanson J.A., Yang H., Nixon B.T.
    Structure 18:1420-1430(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 122-387 IN COMPLEX WITH ATP.
  5. "Structure, function, and tethering of DNA-binding domains in sigma(54) transcriptional activators."
    Vidangos N., Maris A.E., Young A., Hong E., Pelton J.G., Batchelor J.D., Wemmer D.E.
    Biopolymers 99:1082-1096(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.34 ANGSTROMS) OF 393-438, DISULFIDE BONDS.
  6. "Nucleotide-induced asymmetry within ATPase activator ring drives sigma54-RNAP interaction and ATP hydrolysis."
    Sysoeva T.A., Chowdhury S., Guo L., Nixon B.T.
    Genes Dev. 27:2500-2511(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.21 ANGSTROMS) OF 121-387 IN COMPLEX WITH ADP.
  7. "MuB is an AAA+ ATPase that forms helical filaments to control target selection for DNA transposition."
    Mizuno N., Dramicanin M., Mizuuchi M., Adam J., Wang Y., Han Y.W., Yang W., Steven A.C., Mizuuchi K., Ramon-Maiques S.
    Proc. Natl. Acad. Sci. U.S.A. 110:E2441-E2450(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (16.00 ANGSTROMS) OF 312-384 AND 137-309 IN COMPLEX WITH ADP.

Entry informationi

Entry nameiO67198_AQUAE
AccessioniPrimary (citable) accession number: O67198
Entry historyi
Integrated into UniProtKB/TrEMBL: August 1, 1998
Last sequence update: August 1, 1998
Last modified: April 13, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference 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.