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Entry version 109 (07 Oct 2020)
Sequence version 3 (24 Nov 2009)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, RNA-binding
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
BSUB:BSU13880-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
PtsGHI operon antiterminator
Alternative name(s):
RNA-binding antitermination protein GlcT
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:glcT
Synonyms:ykwA
Ordered Locus Names:BSU13880
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBacillus subtilis (strain 168)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri224308 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001570 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003889671 – 281PtsGHI operon antiterminatorAdd BLAST281

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei104Phosphohistidine; by EII-GlcPROSITE-ProRule annotation1 Publication1 Publication1
Modified residuei163Phosphohistidine; by EII-Glc1 Publication1
Modified residuei211Phosphohistidine; by HPr1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
O31691

PRoteomics IDEntifications database

More...
PRIDEi
O31691

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O31691

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

STRING: functional protein association networks

More...
STRINGi
224308.BSU13880

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1281
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
O31691

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
O31691

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O31691

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini69 – 174PRD 1PROSITE-ProRule annotationAdd BLAST106
Domaini175 – 278PRD 2PROSITE-ProRule annotationAdd BLAST104

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 60RNA bindingAdd BLAST60

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG3711, Bacteria

KEGG Orthology (KO)

More...
KOi
K03480

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.24.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004341, CAT_RNA-bd_dom
IPR036650, CAT_RNA-bd_dom_sf
IPR011608, PRD
IPR036634, PRD_sf
IPR001550, Transcrpt_antitermin_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03123, CAT_RBD, 1 hit
PF00874, PRD, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01061, CAT_RBD, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50151, SSF50151, 1 hit
SSF63520, SSF63520, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00654, PRD_1, 1 hit
PS51372, PRD_2, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iED76E0D547760BDA
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Y11193 Genomic DNA Translation: CAA72077.1
AL009126 Genomic DNA Translation: CAB13261.2 Different initiation.

Protein sequence database of the Protein Information Resource

More...
PIRi
D69632

NCBI Reference Sequences

More...
RefSeqi
NP_389271.2, NC_000964.3

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAB13261; CAB13261; BSU13880

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
939254

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bsu:BSU13880

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|224308.43.peg.1471

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GWHX-ray1.95A/B171-273[»]
3RIOX-ray1.99A2-170[»]
3UFEX-ray1.50A/B171-273[»]
BMRBiO31691
SMRiO31691
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU13880

PTM databases

iPTMnetiO31691

Proteomic databases

PaxDbiO31691
PRIDEiO31691

Genome annotation databases

EnsemblBacteriaiCAB13261; CAB13261; BSU13880
GeneIDi939254
KEGGibsu:BSU13880
PATRICifig|224308.43.peg.1471

Phylogenomic databases

eggNOGiCOG3711, Bacteria
KOiK03480

Enzyme and pathway databases

BioCyciBSUB:BSU13880-MONOMER

Miscellaneous databases

EvolutionaryTraceiO31691

Family and domain databases

Gene3Di2.30.24.10, 1 hit
InterProiView protein in InterPro
IPR004341, CAT_RNA-bd_dom
IPR036650, CAT_RNA-bd_dom_sf
IPR011608, PRD
IPR036634, PRD_sf
IPR001550, Transcrpt_antitermin_CS
PfamiView protein in Pfam
PF03123, CAT_RBD, 1 hit
PF00874, PRD, 2 hits
SMARTiView protein in SMART
SM01061, CAT_RBD, 1 hit
SUPFAMiSSF50151, SSF50151, 1 hit
SSF63520, SSF63520, 2 hits
PROSITEiView protein in PROSITE
PS00654, PRD_1, 1 hit
PS51372, PRD_2, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGLCT_BACSU
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O31691
Secondary accession number(s): O06710
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: November 24, 2009
Last modified: October 7, 2020
This is version 109 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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
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