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Protein

PtsGHI operon antiterminator

Gene

glcT

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mediates the positive regulation of the glucose PTS operon (ptsGHI) by functioning as an antiterminator factor of transcription via its interaction with the RNA-antiterminator (RAT) sequence located upstream of the ptsG gene. The RNA-binding domain of GlcT directly binds to the RNA antiterminator (RAT) sequence and prevents transcriptional termination. GlcT binding requires two identical and nearly symmetrical triple base pairings in the RAT sequence.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciBSUB:BSU13880-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
PtsGHI operon antiterminator
Alternative name(s):
RNA-binding antitermination protein GlcT
Gene namesi
Name:glcT
Synonyms:ykwA
Ordered Locus Names:BSU13880
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi5F → L: Loss of antiterminator activity; when associated with P-19. 1 Publication1
Mutagenesisi5F → S: Loss of antiterminator activity; when associated with T-29. 1 Publication1
Mutagenesisi9K → R: Drastically reduced antiterminator activity; when associated with N-38. 1 Publication1
Mutagenesisi10V → G: Loss of antiterminator activity. 1 Publication1
Mutagenesisi11L → P: Drastically reduced antiterminator activity. 1 Publication1
Mutagenesisi12N → D: Loss of antiterminator activity. 1 Publication1
Mutagenesisi19S → P: Loss of antiterminator activity; when associated with L-5. 1 Publication1
Mutagenesisi20H → R: Drastically reduced antiterminator activity. 1 Publication1
Mutagenesisi29I → T: Loss of antiterminator activity; when associated with S-5. 1 Publication1
Mutagenesisi38K → N: Drastically reduced antiterminator activity; when associated with R-9. 1 Publication1
Mutagenesisi51M → T: Drastically reduced antiterminator activity. 1 Publication1
Mutagenesisi52F → V: Loss of antiterminator activity. 1 Publication1
Mutagenesisi102T → S: Affects negative regulation of the antiterminator activity; when associated with T-103. 1 Publication1
Mutagenesisi103D → T: Affects negative regulation of the antiterminator activity; when associated with S-102. 1 Publication1
Mutagenesisi104H → A: Affects negative regulation of the antiterminator activity. No effect on phosphorylation by HPr. Abolishes phosphorylation by both HPr and EII-Glc; when associated with D-211. 2 Publications1
Mutagenesisi104H → D: Affects negative regulation of the antitermination activity. 2 Publications1
Mutagenesisi109I → Q: No effect on negative regulation of the antiterminator activity. 1 Publication1
Mutagenesisi163H → D: Affects negative regulation of the antiterminator activity. No effect on phosphorylation by HPr. Abolishes phosphorylation by both HPr and EII-Glc; when associated with D-211. 1 Publication1
Mutagenesisi211H → D: Strongly reduced phosphorylation by HPr. Abolishes phosphorylation by both HPr and EII-Glc; when associated with A-104 or D-163. 1 Publication1
Mutagenesisi245T → P: Loss of ptsG expression. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003889671 – 281PtsGHI operon antiterminatorAdd BLAST281

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei104Phosphohistidine; by EII-GlcPROSITE-ProRule annotation1 Publication1
Modified residuei163Phosphohistidine; by EII-Glc1 Publication1
Modified residuei211Phosphohistidine; by HPr1 Publication1

Post-translational modificationi

Phosphorylated by HPr (PtsH) and EII-Glc (PtsG). HPr phosphorylates the PRD 2 domain which has a slight stimulatory effect on GlcT activity, while EII-Glc phosphorylates the PRD 1 domain which inactivates GlcT. The phosphorylation is dependent on the presence or absence of glucose which acts as an inducer of the ptsGHI operon expression. In the presence of glucose the phosphoryl group is transferred from phosphorylated HPr to the sugar via EII-Glc. Under these conditions GlcT is not phosphorylated and binds to the RAT sequence, thus allowing transcription of the ptsGHI operon. In the absence of glucose, phosphorylated EII-Glc accumulates in the cell and phosphorylates the PRD 1 domain of GlcT, leading to its inactivation; this phosphorylation may prevent dimerization of GlcT.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO31691.
PRIDEiO31691.

PTM databases

iPTMnetiO31691.

Interactioni

Subunit structurei

Homodimer (By similarity). The monomeric form probably also exists but it would be inactive in RNA binding and antitermination.By similarity

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100007706.

Structurei

Secondary structure

1281
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 12Combined sources9
Beta strandi15 – 19Combined sources5
Helixi21 – 23Combined sources3
Beta strandi25 – 29Combined sources5
Turni31 – 36Combined sources6
Beta strandi42 – 44Combined sources3
Beta strandi47 – 49Combined sources3
Beta strandi52 – 54Combined sources3
Helixi57 – 66Combined sources10
Turni67 – 69Combined sources3
Helixi72 – 89Combined sources18
Helixi97 – 113Combined sources17
Helixi123 – 129Combined sources7
Helixi131 – 148Combined sources18
Helixi156 – 169Combined sources14
Helixi173 – 175Combined sources3
Helixi180 – 194Combined sources15
Helixi203 – 221Combined sources19
Helixi229 – 238Combined sources10
Helixi240 – 257Combined sources18
Helixi264 – 273Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GWHX-ray1.95A/B171-273[»]
3RIOX-ray1.99A2-170[»]
3UFEX-ray1.50A/B171-273[»]
ProteinModelPortaliO31691.
SMRiO31691.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO31691.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini69 – 174PRD 1PROSITE-ProRule annotationAdd BLAST106
Domaini175 – 278PRD 2PROSITE-ProRule annotationAdd BLAST104

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 60RNA bindingAdd BLAST60

Domaini

Composed of 3 domains: an N-terminal RNA-binding domain that prevents transcriptional termination, and two PTS regulation domains, PRD 1 and PRD 2. PRD 1 is the target of negative control exerted by EII-Glc and PRD 2 is the target of HPr.

Sequence similaritiesi

Contains 2 PRD domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CID. Bacteria.
COG3711. LUCA.
HOGENOMiHOG000223756.
KOiK03480.

Family and domain databases

Gene3Di1.10.1790.10. 2 hits.
2.30.24.10. 1 hit.
InterProiIPR004341. CAT_RNA-bd_dom.
IPR011608. PRD.
IPR001550. Transcrpt_antitermin_CS.
[Graphical view]
PfamiPF03123. CAT_RBD. 1 hit.
PF00874. PRD. 2 hits.
[Graphical view]
SMARTiSM01061. CAT_RBD. 1 hit.
[Graphical view]
SUPFAMiSSF50151. SSF50151. 1 hit.
SSF63520. SSF63520. 2 hits.
PROSITEiPS00654. PRD_1. 1 hit.
PS51372. PRD_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O31691-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGSFTVKKV LNNNVLIASH HKYSEVVLIG KGIGFGKKQD DVIEDKGYDK
60 70 80 90 100
MFILKDEKEQ KQFKKLLDYV DEKLVDISND VIYHISNRTN HSLNEHIHIA
110 120 130 140 150
LTDHIAFAIK RQQQGFDMKN PFLMETQSLY PEEYQIAKEV IDMINEKAGL
160 170 180 190 200
CLPEGEIGFI ALHIHSALTN RPLSEVNQHS QLMAQLVEVI EDSFQMKVNK
210 220 230 240 250
ESVNYLRLIR HIRFTIERIK KEEPTKEPEK LMLLLKNEYP LCYNTAWKLI
260 270 280
KILQQTLKKP VHEAEAVYLT LHLYRLTNKI S
Length:281
Mass (Da):32,755
Last modified:November 24, 2009 - v3
Checksum:iED76E0D547760BDA
GO

Sequence cautioni

The sequence CAB13261 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11193 Genomic DNA. Translation: CAA72077.1.
AL009126 Genomic DNA. Translation: CAB13261.2. Different initiation.
PIRiD69632.
RefSeqiNP_389271.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13261; CAB13261; BSU13880.
GeneIDi939254.
KEGGibsu:BSU13880.
PATRICi18974559. VBIBacSub10457_1471.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11193 Genomic DNA. Translation: CAA72077.1.
AL009126 Genomic DNA. Translation: CAB13261.2. Different initiation.
PIRiD69632.
RefSeqiNP_389271.2. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GWHX-ray1.95A/B171-273[»]
3RIOX-ray1.99A2-170[»]
3UFEX-ray1.50A/B171-273[»]
ProteinModelPortaliO31691.
SMRiO31691.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100007706.

PTM databases

iPTMnetiO31691.

Proteomic databases

PaxDbiO31691.
PRIDEiO31691.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13261; CAB13261; BSU13880.
GeneIDi939254.
KEGGibsu:BSU13880.
PATRICi18974559. VBIBacSub10457_1471.

Phylogenomic databases

eggNOGiENOG4105CID. Bacteria.
COG3711. LUCA.
HOGENOMiHOG000223756.
KOiK03480.

Enzyme and pathway databases

BioCyciBSUB:BSU13880-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO31691.

Family and domain databases

Gene3Di1.10.1790.10. 2 hits.
2.30.24.10. 1 hit.
InterProiIPR004341. CAT_RNA-bd_dom.
IPR011608. PRD.
IPR001550. Transcrpt_antitermin_CS.
[Graphical view]
PfamiPF03123. CAT_RBD. 1 hit.
PF00874. PRD. 2 hits.
[Graphical view]
SMARTiSM01061. CAT_RBD. 1 hit.
[Graphical view]
SUPFAMiSSF50151. SSF50151. 1 hit.
SSF63520. SSF63520. 2 hits.
PROSITEiPS00654. PRD_1. 1 hit.
PS51372. PRD_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGLCT_BACSU
AccessioniPrimary (citable) accession number: O31691
Secondary accession number(s): O06710
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: November 24, 2009
Last modified: November 2, 2016
This is version 96 of the entry and version 3 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.