TAGF_BACSU
ID TAGF_BACSU Reviewed; 746 AA.
AC P13485;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Teichoic acid poly(glycerol phosphate) polymerase {ECO:0000305};
DE EC=2.7.8.12 {ECO:0000269|PubMed:12637499, ECO:0000269|PubMed:16141206, ECO:0000269|PubMed:18465758, ECO:0000269|PubMed:19520862};
DE AltName: Full=CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase;
DE AltName: Full=CGPTase;
DE AltName: Full=Major teichoic acid biosynthesis protein F;
DE AltName: Full=Poly(glycerol phosphate) polymerase {ECO:0000303|PubMed:12637499};
DE AltName: Full=Tag polymerase;
GN Name=tagF; Synonyms=rodC, tag3; OrderedLocusNames=BSU35720;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT RODC1.
RC STRAIN=168;
RX PubMed=2507871; DOI=10.1111/j.1365-2958.1989.tb00276.x;
RA Honeyman A.L., Stewart G.C.;
RT "The nucleotide sequence of the rodC operon of Bacillus subtilis.";
RL Mol. Microbiol. 3:1257-1268(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION.
RC STRAIN=168;
RX PubMed=1309530; DOI=10.1128/jb.174.2.646-649.1992;
RA Pooley H.M., Abellan F.-X., Karamata D.;
RT "CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase, which is
RT involved in the synthesis of the major wall teichoic acid in Bacillus
RT subtilis 168, is encoded by tagF (rodC).";
RL J. Bacteriol. 174:646-649(1992).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=168 / EB6;
RX PubMed=12637499; DOI=10.1074/jbc.m300706200;
RA Schertzer J.W., Brown E.D.;
RT "Purified, recombinant TagF protein from Bacillus subtilis 168 catalyzes
RT the polymerization of glycerol phosphate onto a membrane acceptor in
RT vitro.";
RL J. Biol. Chem. 278:18002-18007(2003).
RN [5]
RP REGULATION BY WALR/WALK.
RX PubMed=12950927; DOI=10.1046/j.1365-2958.2003.03661.x;
RA Howell A., Dubrac S., Andersen K.K., Noone D., Fert J., Msadek T.,
RA Devine K.;
RT "Genes controlled by the essential YycG/YycF two-component system of
RT Bacillus subtilis revealed through a novel hybrid regulator approach.";
RL Mol. Microbiol. 49:1639-1655(2003).
RN [6]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP HIS-474; GLU-604; HIS-612; ASP-630; GLU-639; ASP-645 AND ASP-650.
RC STRAIN=168 / EB6;
RX PubMed=16141206; DOI=10.1074/jbc.m507153200;
RA Schertzer J.W., Bhavsar A.P., Brown E.D.;
RT "Two conserved histidine residues are critical to the function of the TagF-
RT like family of enzymes.";
RL J. Biol. Chem. 280:36683-36690(2005).
RN [7]
RP CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=18465758; DOI=10.1002/cbic.200800026;
RA Pereira M.P., Schertzer J.W., D'Elia M.A., Koteva K.P., Hughes D.W.,
RA Wright G.D., Brown E.D.;
RT "The wall teichoic acid polymerase TagF efficiently synthesizes
RT poly(glycerol phosphate) on the TagB product lipid III.";
RL ChemBioChem 9:1385-1390(2008).
RN [8]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP AND REACTION MECHANISM.
RC STRAIN=168 / EB6;
RX PubMed=19520862; DOI=10.1074/jbc.m109.010215;
RA Sewell E.W., Pereira M.P., Brown E.D.;
RT "The wall teichoic acid polymerase TagF is non-processive in vitro and
RT amenable to study using steady state kinetic analysis.";
RL J. Biol. Chem. 284:21132-21138(2009).
CC -!- FUNCTION: Responsible for the polymerization of the main chain of the
CC major teichoic acid by sequential transfer of glycerol phosphate units
CC from CDP-glycerol to the disaccharide linkage unit. Synthesizes
CC polymers of approximately 35 glycerol phosphate units in length.
CC {ECO:0000269|PubMed:12637499, ECO:0000269|PubMed:1309530}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-O-[(2R)-glycerylphospho]-N-acetyl-beta-D-mannosaminyl-
CC (1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl
CC diphosphate + n CDP-glycerol = 4-O-{[(2R)-1-glycerylphospho](n)-(2R)-
CC 1-glycerylphospho}-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-
CC alpha-D-glucosaminyl undecaprenyl diphosphate + n CMP + n H(+);
CC Xref=Rhea:RHEA:13565, Rhea:RHEA-COMP:12597, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58311, ChEBI:CHEBI:60377, ChEBI:CHEBI:132211,
CC ChEBI:CHEBI:132224; EC=2.7.8.12;
CC Evidence={ECO:0000269|PubMed:12637499, ECO:0000269|PubMed:16141206,
CC ECO:0000269|PubMed:18465758, ECO:0000269|PubMed:19520862};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=340 uM for CDP-glycerol {ECO:0000269|PubMed:12637499};
CC KM=230 uM for CDP-glycerol {ECO:0000269|PubMed:16141206};
CC KM=152 uM for CDP-glycerol {ECO:0000269|PubMed:19520862};
CC KM=2.6 uM for lipid III analog {ECO:0000269|PubMed:18465758};
CC Note=kcat for CDP-glycerol is 14 min(-1) (PubMed:16141206). kcat for
CC lipid III analog is 26 sec(-1) (PubMed:18465758).
CC {ECO:0000269|PubMed:16141206, ECO:0000269|PubMed:18465758};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:16141206};
CC -!- PATHWAY: Cell wall biogenesis; poly(glycerol phosphate) teichoic acid
CC biosynthesis.
CC -!- INTERACTION:
CC P13485; P27621: tagB; NbExp=3; IntAct=EBI-6401722, EBI-6401730;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC -!- INDUCTION: Positively regulated by WalR. Mainly expressed during
CC exponential growth and rapidly shut off as cells enter the stationary
CC phase.
CC -!- SIMILARITY: Belongs to the CDP-glycerol glycerophosphotransferase
CC family. {ECO:0000305}.
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DR EMBL; X15200; CAA33271.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15589.1; -; Genomic_DNA.
DR PIR; S06049; S06049.
DR RefSeq; NP_391453.1; NC_000964.3.
DR RefSeq; WP_003243463.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P13485; -.
DR SMR; P13485; -.
DR IntAct; P13485; 6.
DR STRING; 224308.BSU35720; -.
DR jPOST; P13485; -.
DR PaxDb; P13485; -.
DR PRIDE; P13485; -.
DR EnsemblBacteria; CAB15589; CAB15589; BSU_35720.
DR GeneID; 936803; -.
DR KEGG; bsu:BSU35720; -.
DR PATRIC; fig|224308.179.peg.3867; -.
DR eggNOG; COG1887; Bacteria.
DR InParanoid; P13485; -.
DR OMA; ENTVIKC; -.
DR PhylomeDB; P13485; -.
DR BioCyc; BSUB:BSU35720-MON; -.
DR BioCyc; MetaCyc:BSU35720-MON; -.
DR SABIO-RK; P13485; -.
DR UniPathway; UPA00827; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047355; F:CDP-glycerol glycerophosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0019350; P:teichoic acid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.11820; -; 1.
DR Gene3D; 3.40.50.12580; -; 1.
DR InterPro; IPR007554; Glycerophosphate_synth.
DR InterPro; IPR043148; TagF_C.
DR InterPro; IPR043149; TagF_N.
DR Pfam; PF04464; Glyphos_transf; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Membrane;
KW Reference proteome; Teichoic acid biosynthesis; Transferase.
FT CHAIN 1..746
FT /note="Teichoic acid poly(glycerol phosphate) polymerase"
FT /id="PRO_0000072422"
FT BINDING 473..477
FT /ligand="CDP-glycerol"
FT /ligand_id="ChEBI:CHEBI:58311"
FT /evidence="ECO:0000250|UniProtKB:Q5HLM5"
FT BINDING 540
FT /ligand="CDP-glycerol"
FT /ligand_id="ChEBI:CHEBI:58311"
FT /evidence="ECO:0000250|UniProtKB:Q5HLM5"
FT BINDING 573..574
FT /ligand="CDP-glycerol"
FT /ligand_id="ChEBI:CHEBI:58311"
FT /evidence="ECO:0000250|UniProtKB:Q5HLM5"
FT BINDING 610..612
FT /ligand="CDP-glycerol"
FT /ligand_id="ChEBI:CHEBI:58311"
FT /evidence="ECO:0000250|UniProtKB:Q5HLM5"
FT BINDING 652..653
FT /ligand="CDP-glycerol"
FT /ligand_id="ChEBI:CHEBI:58311"
FT /evidence="ECO:0000250|UniProtKB:Q5HLM5"
FT BINDING 657
FT /ligand="CDP-glycerol"
FT /ligand_id="ChEBI:CHEBI:58311"
FT /evidence="ECO:0000250|UniProtKB:Q5HLM5"
FT VARIANT 644
FT /note="S -> F (in mutant rodC1; temperature-sensitive)"
FT MUTAGEN 474
FT /note="H->A: No activity."
FT /evidence="ECO:0000269|PubMed:16141206"
FT MUTAGEN 604
FT /note="E->A: No effect on catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:16141206"
FT MUTAGEN 612
FT /note="H->A: No activity."
FT /evidence="ECO:0000269|PubMed:16141206"
FT MUTAGEN 630
FT /note="D->A: 3-fold reduction in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:16141206"
FT MUTAGEN 639
FT /note="E->A: 4-fold reduction in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:16141206"
FT MUTAGEN 645
FT /note="D->A: 3-fold reduction in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:16141206"
FT MUTAGEN 650
FT /note="D->A: Did not get expressed in heterologous host."
FT /evidence="ECO:0000269|PubMed:16141206"
SQ 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
