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Teichoic acid poly(glycerol phosphate) polymerase (EC 2.7.8.12) (CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase) (CGPTase) (Major teichoic acid biosynthesis protein F) (Poly(glycerol phosphate) polymerase) (Tag polymerase)

 TAGF_BACSU              Reviewed;         746 AA.
P13485;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
28-FEB-2018, entry version 127.
RecName: Full=Teichoic acid poly(glycerol phosphate) polymerase {ECO:0000305};
EC=2.7.8.12 {ECO:0000269|PubMed:12637499, ECO:0000269|PubMed:16141206, ECO:0000269|PubMed:18465758, ECO:0000269|PubMed:19520862};
AltName: Full=CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase;
AltName: Full=CGPTase;
AltName: Full=Major teichoic acid biosynthesis protein F;
AltName: Full=Poly(glycerol phosphate) polymerase {ECO:0000303|PubMed:12637499};
AltName: Full=Tag polymerase;
Name=tagF; Synonyms=rodC, tag3; OrderedLocusNames=BSU35720;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT RODC1.
STRAIN=168;
PubMed=2507871; DOI=10.1111/j.1365-2958.1989.tb00276.x;
Honeyman A.L., Stewart G.C.;
"The nucleotide sequence of the rodC operon of Bacillus subtilis.";
Mol. Microbiol. 3:1257-1268(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[3]
FUNCTION.
STRAIN=168;
PubMed=1309530; DOI=10.1128/jb.174.2.646-649.1992;
Pooley H.M., Abellan F.-X., Karamata D.;
"CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase, which
is involved in the synthesis of the major wall teichoic acid in
Bacillus subtilis 168, is encoded by tagF (rodC).";
J. Bacteriol. 174:646-649(1992).
[4]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=168 / EB6;
PubMed=12637499; DOI=10.1074/jbc.M300706200;
Schertzer J.W., Brown E.D.;
"Purified, recombinant TagF protein from Bacillus subtilis 168
catalyzes the polymerization of glycerol phosphate onto a membrane
acceptor in vitro.";
J. Biol. Chem. 278:18002-18007(2003).
[5]
REGULATION BY WALR/WALK.
PubMed=12950927; DOI=10.1046/j.1365-2958.2003.03661.x;
Howell A., Dubrac S., Andersen K.K., Noone D., Fert J., Msadek T.,
Devine K.;
"Genes controlled by the essential YycG/YycF two-component system of
Bacillus subtilis revealed through a novel hybrid regulator
approach.";
Mol. Microbiol. 49:1639-1655(2003).
[6]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
HIS-474; GLU-604; HIS-612; ASP-630; GLU-639; ASP-645 AND ASP-650.
STRAIN=168 / EB6;
PubMed=16141206; DOI=10.1074/jbc.M507153200;
Schertzer J.W., Bhavsar A.P., Brown E.D.;
"Two conserved histidine residues are critical to the function of the
TagF-like family of enzymes.";
J. Biol. Chem. 280:36683-36690(2005).
[7]
CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
PubMed=18465758; DOI=10.1002/cbic.200800026;
Pereira M.P., Schertzer J.W., D'Elia M.A., Koteva K.P., Hughes D.W.,
Wright G.D., Brown E.D.;
"The wall teichoic acid polymerase TagF efficiently synthesizes
poly(glycerol phosphate) on the TagB product lipid III.";
ChemBioChem 9:1385-1390(2008).
[8]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
SPECIFICITY, AND REACTION MECHANISM.
STRAIN=168 / EB6;
PubMed=19520862; DOI=10.1074/jbc.M109.010215;
Sewell E.W., Pereira M.P., Brown E.D.;
"The wall teichoic acid polymerase TagF is non-processive in vitro and
amenable to study using steady state kinetic analysis.";
J. Biol. Chem. 284:21132-21138(2009).
-!- FUNCTION: 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. {ECO:0000269|PubMed:12637499,
ECO:0000269|PubMed:1309530}.
-!- CATALYTIC ACTIVITY: n CDP-glycerol + 4-O-((2R)-glycerophospho)-N-
acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-
diphospho-ditrans,octacis-undecaprenol = n CMP + 4-O-(((2R)-
glycerophospho)n-(2R)-glycerophospho)-N-acetyl-beta-D-
mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-
ditrans,octacis-undecaprenol. {ECO:0000269|PubMed:12637499,
ECO:0000269|PubMed:16141206, ECO:0000269|PubMed:18465758,
ECO:0000269|PubMed:19520862}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=340 uM for CDP-glycerol {ECO:0000269|PubMed:12637499};
KM=230 uM for CDP-glycerol {ECO:0000269|PubMed:16141206};
KM=152 uM for CDP-glycerol {ECO:0000269|PubMed:19520862};
KM=2.6 uM for lipid III analog {ECO:0000269|PubMed:18465758};
Note=kcat for CDP-glycerol is 14 min(-1) (PubMed:16141206). kcat
for lipid III analog is 26 sec(-1) (PubMed:18465758).
{ECO:0000269|PubMed:16141206, ECO:0000269|PubMed:18465758};
pH dependence:
Optimum pH is 8. {ECO:0000269|PubMed:16141206};
-!- PATHWAY: Cell wall biogenesis; poly(glycerol phosphate) teichoic
acid biosynthesis.
-!- INTERACTION:
P27621:tagB; NbExp=3; IntAct=EBI-6401722, EBI-6401730;
-!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
-!- INDUCTION: Positively regulated by WalR. Mainly expressed during
exponential growth and rapidly shut off as cells enter the
stationary phase.
-!- SIMILARITY: Belongs to the CDP-glycerol glycerophosphotransferase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X15200; CAA33271.1; -; Genomic_DNA.
EMBL; AL009126; CAB15589.1; -; Genomic_DNA.
PIR; S06049; S06049.
RefSeq; NP_391453.1; NC_000964.3.
RefSeq; WP_003243463.1; NZ_JNCM01000034.1.
ProteinModelPortal; P13485; -.
SMR; P13485; -.
IntAct; P13485; 6.
STRING; 224308.Bsubs1_010100019326; -.
PaxDb; P13485; -.
PRIDE; P13485; -.
EnsemblBacteria; CAB15589; CAB15589; BSU35720.
GeneID; 936803; -.
KEGG; bsu:BSU35720; -.
PATRIC; fig|224308.179.peg.3867; -.
eggNOG; ENOG4107SJB; Bacteria.
eggNOG; COG1887; LUCA.
HOGENOM; HOG000009147; -.
InParanoid; P13485; -.
KO; K09809; -.
OMA; KFCYLES; -.
PhylomeDB; P13485; -.
BioCyc; BSUB:BSU35720-MONOMER; -.
BioCyc; MetaCyc:BSU35720-MONOMER; -.
SABIO-RK; P13485; -.
UniPathway; UPA00827; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0047355; F:CDP-glycerol glycerophosphotransferase activity; IEA:UniProtKB-EC.
GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IBA:GO_Central.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0019350; P:teichoic acid biosynthetic process; IEA:UniProtKB-KW.
InterPro; IPR007554; Glycerophosphate_synth.
Pfam; PF04464; Glyphos_transf; 1.
1: Evidence at protein level;
Cell membrane; Cell wall biogenesis/degradation; Complete proteome;
Membrane; Reference proteome; Teichoic acid biosynthesis; Transferase.
CHAIN 1 746 Teichoic acid poly(glycerol phosphate)
polymerase.
/FTId=PRO_0000072422.
REGION 473 477 CDP-glycerol binding.
{ECO:0000250|UniProtKB:Q5HLM5}.
REGION 573 574 CDP-glycerol binding.
{ECO:0000250|UniProtKB:Q5HLM5}.
REGION 610 612 CDP-glycerol binding.
{ECO:0000250|UniProtKB:Q5HLM5}.
REGION 652 653 CDP-glycerol binding.
{ECO:0000250|UniProtKB:Q5HLM5}.
BINDING 540 540 CDP-glycerol.
{ECO:0000250|UniProtKB:Q5HLM5}.
BINDING 657 657 CDP-glycerol.
{ECO:0000250|UniProtKB:Q5HLM5}.
VARIANT 644 644 S -> F (in mutant rodC1; temperature-
sensitive).
MUTAGEN 474 474 H->A: No activity.
{ECO:0000269|PubMed:16141206}.
MUTAGEN 604 604 E->A: No effect on catalytic efficiency.
{ECO:0000269|PubMed:16141206}.
MUTAGEN 612 612 H->A: No activity.
{ECO:0000269|PubMed:16141206}.
MUTAGEN 630 630 D->A: 3-fold reduction in catalytic
efficiency.
{ECO:0000269|PubMed:16141206}.
MUTAGEN 639 639 E->A: 4-fold reduction in catalytic
efficiency.
{ECO:0000269|PubMed:16141206}.
MUTAGEN 645 645 D->A: 3-fold reduction in catalytic
efficiency.
{ECO:0000269|PubMed:16141206}.
MUTAGEN 650 650 D->A: Did not get expressed in
heterologous host.
{ECO:0000269|PubMed:16141206}.
SEQUENCE 746 AA; 88063 MW; 9FEB94D83332B980 CRC64;
MSLVVDTNKR KQKGKSFYTE EQKKVMIENT VIKCILKSLK NNLGSLELLI SIDSEHQFLE
DYQLFLKLKE RRSGTESEFP LQNTGSLEYK TEINAHVLPM PVEMGQTYDF YVEFRKKYED
AEQEPLLKRL SAEVNSIERA FHVDQTTELL ILPYTTDKGN FSIKVKREAK IIRFDQIEIS
SEEISITGYA GYLSSENQYR IKNLNLILKK GGETPIEEKF PIKLERKTHG LENMRADGFV
PELYDFEVKV PLKEIPFSNE KRYVYRLFME YICNDDEGTD IQFNSTALVL GDRKNKLKGL
VSIIKTNNAP VRYEVFKKKK KQTLGIRVND YSLKTRMKYF IKGKKKRLVS KIKKITKMRN
KLITKTYKSL FMMASRMPVK RKTVIFESFN GKQYSCNPRA IYEYMRENHP EYKMYWSVNK
QYSAPFDEKG IPYINRLSLK WLFAMARAEY WVVNSRLPLW IPKPSHTTYL QTWHGTPLKR
LAMDMEEVHM PGTNTKKYKR NFIKEASNWD YLISPNGYST EIFTRAFQFN KTMIESGYPR
NDFLHNDNNE ETISLIKSRL NIPRDKKVIL YAPTWRDDQF YAKGRYKFDL DLDLHQLRQE
LGNEYIVILR MHYLVAENFD LGPFEGFAYD FSAYEDIREL YMVSDLLITD YSSVFFDFAN
LKRPMLFFVP DIETYRDKLR GFYFDFEKEA PGPLVKTTEE TIEAIKQISS PDYKLPVSFG
PFYDKFCYLE SGRSSEKVVN TVFKAE


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