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UniProtKB - P13485 (TAGF_BACSU)
Protein
Teichoic acid poly(glycerol phosphate) polymerase
Gene
tagF
Organism
Bacillus subtilis (strain 168)
Status
Functioni
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.
2 PublicationsCatalytic activityi
- 4-O-[(2R)-glycerylphospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + n CDP-glycerol = 4-O-{[(2R)-1-glycerylphospho](n)-(2R)-1-glycerylphospho}-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl undecaprenyl diphosphate + n CMP + n H+4 PublicationsEC:2.7.8.124 Publications
Kineticsi
kcat for CDP-glycerol is 14 min(-1) (PubMed:16141206). kcat for lipid III analog is 26 sec(-1) (PubMed:18465758).2 Publications
- KM=340 µM for CDP-glycerol1 Publication
- KM=230 µM for CDP-glycerol1 Publication
- KM=152 µM for CDP-glycerol1 Publication
- KM=2.6 µM for lipid III analog1 Publication
pH dependencei
Optimum pH is 8.1 Publication
: poly(glycerol phosphate) teichoic acid biosynthesis Pathwayi
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 540 | CDP-glycerolBy similarity | 1 | |
Binding sitei | 657 | CDP-glycerolBy similarity | 1 |
GO - Molecular functioni
- CDP-glycerol glycerophosphotransferase activity Source: UniProtKB-EC
GO - Biological processi
- cell wall organization Source: UniProtKB-KW
- teichoic acid biosynthetic process Source: UniProtKB-KW
Keywordsi
Molecular function | Transferase |
Biological process | Cell wall biogenesis/degradation, Teichoic acid biosynthesis |
Enzyme and pathway databases
BioCyci | BSUB:BSU35720-MONOMER |
SABIO-RKi | P13485 |
UniPathwayi | UPA00827 |
Names & Taxonomyi
Protein namesi | Recommended name: Teichoic acid poly(glycerol phosphate) polymeraseCurated (EC:2.7.8.124 Publications)Alternative name(s): CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase CGPTase Major teichoic acid biosynthesis protein F Poly(glycerol phosphate) polymerase1 Publication Tag polymerase |
Gene namesi | Name:tagF Synonyms:rodC, tag3 Ordered Locus Names:BSU35720 |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
Subcellular locationi
Plasma membrane
Plasma Membrane
- plasma membrane Source: UniProtKB-SubCell
Keywords - Cellular componenti
Cell membrane, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 474 | H → A: No activity. 1 Publication | 1 | |
Mutagenesisi | 604 | E → A: No effect on catalytic efficiency. 1 Publication | 1 | |
Mutagenesisi | 612 | H → A: No activity. 1 Publication | 1 | |
Mutagenesisi | 630 | D → A: 3-fold reduction in catalytic efficiency. 1 Publication | 1 | |
Mutagenesisi | 639 | E → A: 4-fold reduction in catalytic efficiency. 1 Publication | 1 | |
Mutagenesisi | 645 | D → A: 3-fold reduction in catalytic efficiency. 1 Publication | 1 | |
Mutagenesisi | 650 | D → A: Did not get expressed in heterologous host. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000072422 | 1 – 746 | Teichoic acid poly(glycerol phosphate) polymeraseAdd BLAST | 746 |
Proteomic databases
jPOSTi | P13485 |
PaxDbi | P13485 |
Expressioni
Inductioni
Positively regulated by WalR. Mainly expressed during exponential growth and rapidly shut off as cells enter the stationary phase.
Interactioni
Binary interactionsi
P13485
With | #Exp. | IntAct |
---|---|---|
tagB [P27621] | 3 | EBI-6401722,EBI-6401730 |
Protein-protein interaction databases
IntActi | P13485, 6 interactors |
STRINGi | 224308.BSU35720 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 473 – 477 | CDP-glycerol bindingBy similarity | 5 | |
Regioni | 573 – 574 | CDP-glycerol bindingBy similarity | 2 | |
Regioni | 610 – 612 | CDP-glycerol bindingBy similarity | 3 | |
Regioni | 652 – 653 | CDP-glycerol bindingBy similarity | 2 |
Sequence similaritiesi
Belongs to the CDP-glycerol glycerophosphotransferase family.Curated
Phylogenomic databases
eggNOGi | COG1887, Bacteria |
InParanoidi | P13485 |
OMAi | KFCYLES |
PhylomeDBi | P13485 |
Family and domain databases
Gene3Di | 3.40.50.11820, 1 hit 3.40.50.12580, 1 hit |
InterProi | View protein in InterPro IPR007554, Glycerophosphate_synth IPR043148, TagF_C IPR043149, TagF_N |
Pfami | View protein in Pfam PF04464, Glyphos_transf, 1 hit |
i Sequence
Sequence statusi: Complete.
P13485-1 [UniParc]FASTAAdd to basket
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
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 644 | S → F in mutant rodC1; temperature-sensitive. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X15200 Genomic DNA Translation: CAA33271.1 AL009126 Genomic DNA Translation: CAB15589.1 |
PIRi | S06049 |
RefSeqi | NP_391453.1, NC_000964.3 WP_003243463.1, NZ_JNCM01000034.1 |
Genome annotation databases
EnsemblBacteriai | CAB15589; CAB15589; BSU_35720 |
GeneIDi | 936803 |
KEGGi | bsu:BSU35720 |
PATRICi | fig|224308.179.peg.3867 |
Similar proteinsi
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 |
PIRi | S06049 |
RefSeqi | NP_391453.1, NC_000964.3 WP_003243463.1, NZ_JNCM01000034.1 |
3D structure databases
SMRi | P13485 |
ModBasei | Search... |
Protein-protein interaction databases
IntActi | P13485, 6 interactors |
STRINGi | 224308.BSU35720 |
Proteomic databases
jPOSTi | P13485 |
PaxDbi | P13485 |
Genome annotation databases
EnsemblBacteriai | CAB15589; CAB15589; BSU_35720 |
GeneIDi | 936803 |
KEGGi | bsu:BSU35720 |
PATRICi | fig|224308.179.peg.3867 |
Phylogenomic databases
eggNOGi | COG1887, Bacteria |
InParanoidi | P13485 |
OMAi | KFCYLES |
PhylomeDBi | P13485 |
Enzyme and pathway databases
UniPathwayi | UPA00827 |
BioCyci | BSUB:BSU35720-MONOMER |
SABIO-RKi | P13485 |
Family and domain databases
Gene3Di | 3.40.50.11820, 1 hit 3.40.50.12580, 1 hit |
InterProi | View protein in InterPro IPR007554, Glycerophosphate_synth IPR043148, TagF_C IPR043149, TagF_N |
Pfami | View protein in Pfam PF04464, Glyphos_transf, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | TAGF_BACSU | |
Accessioni | P13485Primary (citable) accession number: P13485 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 1, 1990 |
Last sequence update: | January 1, 1990 | |
Last modified: | February 23, 2022 | |
This is version 142 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families