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Protein

CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase

Gene

tagF

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Is responsible for the polymerization of the main chain of the major teichoic acid by sequential transfer of glycerol phosphate units from CDP-glycerol to the disaccharide linkage unit. Synthesizes polymers of approximately 35 glycerol phosphate units in length.1 Publication

Catalytic activityi

CDP-glycerol + (glycerophosphate)(n) = CMP + (glycerophosphate)(n+1).

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Cell wall biogenesis/degradation, Teichoic acid biosynthesis

Enzyme and pathway databases

BioCyciBSUB:BSU35720-MONOMER.
MetaCyc:MONOMER-8821.
SABIO-RKP13485.
UniPathwayiUPA00827.

Names & Taxonomyi

Protein namesi
Recommended name:
CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase (EC:2.7.8.12)
Alternative name(s):
CGPTase
Major teichoic acid biosynthesis protein F
Polyglycerol phosphate polymerase
Gene namesi
Name:tagF
Synonyms:rodC, tag3
Ordered Locus Names:BSU35720
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 746746CDP-glycerol:poly(glycerophosphate) glycerophosphotransferasePRO_0000072422Add
BLAST

Proteomic databases

PaxDbiP13485.

Expressioni

Inductioni

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

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
tagBP276213EBI-6401722,EBI-6401730

Protein-protein interaction databases

IntActiP13485. 6 interactions.
STRINGi224308.Bsubs1_010100019326.

Structurei

3D structure databases

ProteinModelPortaliP13485.
SMRiP13485. Positions 374-745.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107SJB. Bacteria.
COG1887. LUCA.
HOGENOMiHOG000009147.
InParanoidiP13485.
KOiK09809.
OMAiKFCYLES.
PhylomeDBiP13485.

Family and domain databases

InterProiIPR007554. Glycerophosphate_synth.
[Graphical view]
PfamiPF04464. Glyphos_transf. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13485-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLVVDTNKR KQKGKSFYTE EQKKVMIENT VIKCILKSLK NNLGSLELLI
60 70 80 90 100
SIDSEHQFLE DYQLFLKLKE RRSGTESEFP LQNTGSLEYK TEINAHVLPM
110 120 130 140 150
PVEMGQTYDF YVEFRKKYED AEQEPLLKRL SAEVNSIERA FHVDQTTELL
160 170 180 190 200
ILPYTTDKGN FSIKVKREAK IIRFDQIEIS SEEISITGYA GYLSSENQYR
210 220 230 240 250
IKNLNLILKK GGETPIEEKF PIKLERKTHG LENMRADGFV PELYDFEVKV
260 270 280 290 300
PLKEIPFSNE KRYVYRLFME YICNDDEGTD IQFNSTALVL GDRKNKLKGL
310 320 330 340 350
VSIIKTNNAP VRYEVFKKKK KQTLGIRVND YSLKTRMKYF IKGKKKRLVS
360 370 380 390 400
KIKKITKMRN KLITKTYKSL FMMASRMPVK RKTVIFESFN GKQYSCNPRA
410 420 430 440 450
IYEYMRENHP EYKMYWSVNK QYSAPFDEKG IPYINRLSLK WLFAMARAEY
460 470 480 490 500
WVVNSRLPLW IPKPSHTTYL QTWHGTPLKR LAMDMEEVHM PGTNTKKYKR
510 520 530 540 550
NFIKEASNWD YLISPNGYST EIFTRAFQFN KTMIESGYPR NDFLHNDNNE
560 570 580 590 600
ETISLIKSRL NIPRDKKVIL YAPTWRDDQF YAKGRYKFDL DLDLHQLRQE
610 620 630 640 650
LGNEYIVILR MHYLVAENFD LGPFEGFAYD FSAYEDIREL YMVSDLLITD
660 670 680 690 700
YSSVFFDFAN LKRPMLFFVP DIETYRDKLR GFYFDFEKEA PGPLVKTTEE
710 720 730 740
TIEAIKQISS PDYKLPVSFG PFYDKFCYLE SGRSSEKVVN TVFKAE
Length:746
Mass (Da):88,063
Last modified:January 1, 1990 - v1
Checksum:i9FEB94D83332B980
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti644 – 6441S → F in mutant rodC1; temperature-sensitive.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15200 Genomic DNA. Translation: CAA33271.1.
AL009126 Genomic DNA. Translation: CAB15589.1.
PIRiS06049.
RefSeqiNP_391453.1. NC_000964.3.
WP_003243463.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB15589; CAB15589; BSU35720.
GeneIDi936803.
KEGGibsu:BSU35720.
PATRICi18979160. VBIBacSub10457_3742.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15200 Genomic DNA. Translation: CAA33271.1.
AL009126 Genomic DNA. Translation: CAB15589.1.
PIRiS06049.
RefSeqiNP_391453.1. NC_000964.3.
WP_003243463.1. NZ_JNCM01000034.1.

3D structure databases

ProteinModelPortaliP13485.
SMRiP13485. Positions 374-745.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP13485. 6 interactions.
STRINGi224308.Bsubs1_010100019326.

Proteomic databases

PaxDbiP13485.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15589; CAB15589; BSU35720.
GeneIDi936803.
KEGGibsu:BSU35720.
PATRICi18979160. VBIBacSub10457_3742.

Phylogenomic databases

eggNOGiENOG4107SJB. Bacteria.
COG1887. LUCA.
HOGENOMiHOG000009147.
InParanoidiP13485.
KOiK09809.
OMAiKFCYLES.
PhylomeDBiP13485.

Enzyme and pathway databases

UniPathwayiUPA00827.
BioCyciBSUB:BSU35720-MONOMER.
MetaCyc:MONOMER-8821.
SABIO-RKP13485.

Family and domain databases

InterProiIPR007554. Glycerophosphate_synth.
[Graphical view]
PfamiPF04464. Glyphos_transf. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTAGF_BACSU
AccessioniPrimary (citable) accession number: P13485
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: September 7, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.