Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
We will be switching to the new UniProt website soon. Please explore and share your feedback. Take me to the new website.

UniProtKB - P27623 (TAGD_BACSU)

Entry version 166 (23 Feb 2022)
Sequence version 1 (01 Aug 1992)
Previous versions | rss
Add a publicationFeedback
Protein

Glycerol-3-phosphate cytidylyltransferase

Gene

tagD

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

Catalyzes the transfer of the cytidylyl group of CTP to sn-glycerol 3-phosphate so the activated glycerol 3-phosphate can be used for teichoic acid synthesis, via incorporation into both the linkage unit and the teichoic acid polymer by TagB and TagF.

1 Publication

Miscellaneous

Proceeds via a random order reaction mechanism where there is negative cooperativity in the binding of substrates but not in catalysis.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by the divalent cations cadmium, mercury, tin, copper and zinc.

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=3.85 mM for CTP1 Publication
  2. KM=3.23 mM for glycerol 3-phosphate1 Publication
  1. Vmax=185 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 6.5-9.5.1 Publication

Temperature dependencei

Optimum temperature is 50 degrees Celsius.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: poly(glucopyranosyl N-acetylgalactosamine 1-phosphate) teichoic acid biosynthesis

This protein is involved in the pathway poly(glucopyranosyl N-acetylgalactosamine 1-phosphate) teichoic acid biosynthesis, which is part of Cell wall biogenesis.
View all proteins of this organism that are known to be involved in the pathway poly(glucopyranosyl N-acetylgalactosamine 1-phosphate) teichoic acid biosynthesis and in Cell wall biogenesis.

Pathwayi: poly(glycerol phosphate) teichoic acid biosynthesis

This protein is involved in the pathway poly(glycerol phosphate) teichoic acid biosynthesis, which is part of Cell wall biogenesis.
View all proteins of this organism that are known to be involved in the pathway poly(glycerol phosphate) teichoic acid biosynthesis and in Cell wall biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei44Substrate1 Publication1
Binding sitei46CTP2 Publications1
Binding sitei77Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi9 – 10CTP2 Publications2
Nucleotide bindingi14 – 17CTP2 Publications4
Nucleotide bindingi113 – 120CTP2 Publications8

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionNucleotidyltransferase, Transferase
Biological processCell wall biogenesis/degradation, Teichoic acid biosynthesis

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		BSUB:BSU35740-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.7.39, 658

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00789
UPA00827

<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:
Glycerol-3-phosphate cytidylyltransferase1 Publication (EC:2.7.7.392 Publications)
Short name:
GCT
Short name:
GCTase1 Publication
Short name:
Gro-PCT
Alternative name(s):
CDP-glycerol pyrophosphorylase
Teichoic acid biosynthesis protein D
<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:tagD1 Publication
Ordered Locus Names:BSU35740
<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 lineageiBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›
<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 location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

<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>Mutagenesisi11D → A or E: 0.1% of wild-type activity. 1 Publication1
Mutagenesisi14H → A: Complete loss of activity. 1 Publication1
Mutagenesisi17H → A: Complete loss of activity. 1 Publication1
Mutagenesisi38D → A: 8% of wild-type activity, but 7-fold decrease in substrate affinity. 1 Publication1
Mutagenesisi44K → A: Reduces affinity for glycerol 3-phosphate about 100-fold. 1 Publication1
Mutagenesisi46K → A: Reduces affinity for glycerol 3-phosphate about 100-fold. 1 Publication1
Mutagenesisi55R → A: 0.25% of wild-type activity. 1 Publication1
Mutagenesisi55R → K: 23% of wild-type activity. 1 Publication1
Mutagenesisi63R → A: 14% of wild-type activity. 1 Publication1
Mutagenesisi66D → A: Complete loss of activity, and widespread change in 3D-structure. 1 Publication1
Mutagenesisi66D → E: 16% of wild-type activity. 1 Publication1
Mutagenesisi74W → A: 50% of wild-type activity, but 9-fold decrease in substrate affinity. 1 Publication1
Mutagenesisi84H → A: Complete loss of activity. 1 Publication1
Mutagenesisi94D → A: 18% of wild-type activity, but 100-fold decrease in substrate affinity. 1 Publication1
Mutagenesisi113R → A: 1.75% of wild-type activity. 1 Publication1
Mutagenesisi113R → K: Complete loss of activity. 1 Publication1
Mutagenesisi114T → A: 9% of wild-type activity. 1 Publication1
Mutagenesisi118S → A: 6% of wild-type activity. 1 Publication1
Mutagenesisi119T → A: 8% of wild-type activity. 1 Publication1

Chemistry databases

Drug and drug target database

More...DrugBanki		DB02484, Cytidine 5'-diphosphoglycerol
DB02431, Cytidine-5'-Triphosphate

<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_00002084661 – 129Glycerol-3-phosphate cytidylyltransferaseAdd BLAST129

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P27623

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

More...PaxDbi		P27623

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Positively regulated by WalR. Mainly expressed during exponential growth and rapidly shut off as cells enter the stationary phase.

<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.

2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		224308.BSU35740

<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

1129
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P27623

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		P27623

<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

<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

Belongs to the cytidylyltransferase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0615, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P27623

Identification of Orthologs from Complete Genome Data

More...OMAi		VVYFPYT

Database for complete collections of gene phylogenies

More...PhylomeDBi		P27623

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.620, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR004821, Cyt_trans-like
IPR006409, G3P_cytidylTrfase
IPR014729, Rossmann-like_a/b/a_fold

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01467, CTP_transf_like, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00125, cyt_tran_rel, 1 hit
TIGR01518, g3p_cytidyltrns, 1 hit

<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.

P27623-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKVITYGTF DLLHWGHIKL LERAKQLGDY LVVAISTDEF NLQKQKKAYH 
        60         70         80         90        100
SYEHRKLILE TIRYVDEVIP EKNWEQKKQD IIDHNIDVFV MGDDWEGKFD 
       110        120 
FLKDQCEVVY LPRTEGISTT KIKEEIAGL
Length:129
Mass (Da):15,272
Last modified:August 1, 1992 - v1
<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:iB07F532D9AAE0869
GO

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
M57497 Genomic DNA Translation: AAA22843.1
AL009126 Genomic DNA Translation: CAB15591.1

Protein sequence database of the Protein Information Resource

More...PIRi		A49757

NCBI Reference Sequences

More...RefSeqi		NP_391455.1, NC_000964.3
WP_003227921.1, NZ_JNCM01000034.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		CAB15591; CAB15591; BSU_35740

Database of genes from NCBI RefSeq genomes

More...GeneIDi		936809

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bsu:BSU35740

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|224308.179.peg.3869

<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
M57497 Genomic DNA Translation: AAA22843.1
AL009126 Genomic DNA Translation: CAB15591.1
PIRiA49757
RefSeqiNP_391455.1, NC_000964.3
WP_003227921.1, NZ_JNCM01000034.1

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
1COZX-ray2.00A/B1-129[»]
1N1DX-ray2.00A/B/C/D1-129[»]
SMRiP27623
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU35740

Chemistry databases

DrugBankiDB02484, Cytidine 5'-diphosphoglycerol
DB02431, Cytidine-5'-Triphosphate

Proteomic databases

jPOSTiP27623
PaxDbiP27623

Genome annotation databases

EnsemblBacteriaiCAB15591; CAB15591; BSU_35740
GeneIDi936809
KEGGibsu:BSU35740
PATRICifig|224308.179.peg.3869

Phylogenomic databases

eggNOGiCOG0615, Bacteria
InParanoidiP27623
OMAiVVYFPYT
PhylomeDBiP27623

Enzyme and pathway databases

UniPathwayiUPA00789
UPA00827
BioCyciBSUB:BSU35740-MONOMER
BRENDAi2.7.7.39, 658

Miscellaneous databases

EvolutionaryTraceiP27623

Family and domain databases

Gene3Di3.40.50.620, 1 hit
InterProiView protein in InterPro
IPR004821, Cyt_trans-like
IPR006409, G3P_cytidylTrfase
IPR014729, Rossmann-like_a/b/a_fold
PfamiView protein in Pfam
PF01467, CTP_transf_like, 1 hit
TIGRFAMsiTIGR00125, cyt_tran_rel, 1 hit
TIGR01518, g3p_cytidyltrns, 1 hit

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 nameiTAGD_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: P27623
<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: August 1, 1992
Last sequence update: August 1, 1992
Last modified: February 23, 2022
This is version 166 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again