TAGB_BACSU
ID TAGB_BACSU Reviewed; 381 AA.
AC P27621;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Teichoic acid glycerol-phosphate primase {ECO:0000305};
DE EC=2.7.8.44 {ECO:0000269|PubMed:16150696, ECO:0000269|PubMed:17163636};
DE AltName: Full=CDP-glycerol:N-acetyl-beta-D-mannosaminyl-1,4-N-acetyl-D-glucosaminyldiphosphoundecaprenyl glycerophosphotransferase {ECO:0000303|PubMed:16150696};
DE AltName: Full=CDP-glycerol:glycerophosphate glycerophosphotransferase;
DE AltName: Full=Major teichoic acid biosynthesis protein B;
DE AltName: Full=Tag primase {ECO:0000303|PubMed:16150696};
GN Name=tagB; OrderedLocusNames=BSU35760;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=1906926; DOI=10.1099/00221287-137-4-929;
RA Maueel C., Young M., Karamata D.;
RT "Genes concerned with synthesis of poly(glycerol phosphate), the essential
RT teichoic acid in Bacillus subtilis strain 168, are organized in two
RT divergent transcription units.";
RL J. Gen. Microbiol. 137:929-941(1991).
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 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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP HIS-126.
RX PubMed=16150696; DOI=10.1074/jbc.m507154200;
RA Bhavsar A.P., Truant R., Brown E.D.;
RT "The TagB protein in Bacillus subtilis 168 is an intracellular peripheral
RT membrane protein that can incorporate glycerol phosphate onto a membrane-
RT bound acceptor in vitro.";
RL J. Biol. Chem. 280:36691-36700(2005).
RN [5]
RP CATALYTIC ACTIVITY.
RX PubMed=17163636; DOI=10.1021/cb0500041;
RA Ginsberg C., Zhang Y.H., Yuan Y., Walker S.;
RT "In vitro reconstitution of two essential steps in wall teichoic acid
RT biosynthesis.";
RL ACS Chem. Biol. 1:25-28(2006).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=17660278; DOI=10.1128/jb.00910-07;
RA Bhavsar A.P., D'Elia M.A., Sahakian T.D., Brown E.D.;
RT "The amino terminus of Bacillus subtilis TagB possesses separable
RT localization and functional properties.";
RL J. Bacteriol. 189:6816-6823(2007).
CC -!- FUNCTION: Catalyzes the addition of a single glycerol phosphate residue
CC to the prenoldiphosphate-linked disaccharide, as a primer for
CC polymerisation by TagF. {ECO:0000269|PubMed:16150696}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CDP-glycerol + N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-
CC alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate = 4-
CC O-[(2R)-glycerylphospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-
CC acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl
CC diphosphate + CMP + H(+); Xref=Rhea:RHEA:33815, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58311, ChEBI:CHEBI:60377, ChEBI:CHEBI:132210,
CC ChEBI:CHEBI:132211; EC=2.7.8.44;
CC Evidence={ECO:0000269|PubMed:16150696, ECO:0000269|PubMed:17163636};
CC -!- PATHWAY: Cell wall biogenesis; poly(glycerol phosphate) teichoic acid
CC biosynthesis.
CC -!- INTERACTION:
CC P27621; P13485: tagF; NbExp=3; IntAct=EBI-6401730, EBI-6401722;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16150696,
CC ECO:0000269|PubMed:17660278}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16150696, ECO:0000269|PubMed:17660278}; Cytoplasmic
CC side {ECO:0000269|PubMed:16150696, ECO:0000269|PubMed:17660278}.
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; M57497; AAA22845.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15593.1; -; Genomic_DNA.
DR PIR; C49757; C49757.
DR RefSeq; NP_391457.1; NC_000964.3.
DR RefSeq; WP_009968271.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P27621; -.
DR SMR; P27621; -.
DR IntAct; P27621; 6.
DR STRING; 224308.BSU35760; -.
DR PaxDb; P27621; -.
DR PRIDE; P27621; -.
DR EnsemblBacteria; CAB15593; CAB15593; BSU_35760.
DR GeneID; 936813; -.
DR KEGG; bsu:BSU35760; -.
DR PATRIC; fig|224308.179.peg.3871; -.
DR eggNOG; COG1887; Bacteria.
DR InParanoid; P27621; -.
DR OMA; QVWHANG; -.
DR PhylomeDB; P27621; -.
DR BioCyc; BSUB:BSU35760-MON; -.
DR BioCyc; MetaCyc:BSU35760-MON; -.
DR BRENDA; 2.7.8.44; 658.
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:InterPro.
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..381
FT /note="Teichoic acid glycerol-phosphate primase"
FT /id="PRO_0000208447"
FT MUTAGEN 126
FT /note="H->A: Looses 75% of activity."
FT /evidence="ECO:0000269|PubMed:16150696"
SQ SEQUENCE 381 AA; 44554 MW; 8F89B7659958330D CRC64;
MKIRSLLANC YLYFLSAIAF FLQWVKPESK VTLLISFEAN AKAILEEYEQ GQYSYKLNIL
YTQQASAIAE SFPNVDAYLL QEKNPIHLIK AVYLMFNSKV IITDNYFLLT SVLNKRKQTK
CIQVWHANGS LKKFGLEDIT NMQRTKTDIK RFQKVYSSYD YLTVGSEEMA NIFKKSFGIK
DNQLLKIGVP LTDPYYRENK KKISDTLNIQ RKKIILYAPT FRDYNMQSIQ LPFTEEQLIH
QLKEEYVLFV KLHPAIQNNI DIKYSSDYIK DVSNYALFDL LMAADILITD YSSVPFEFSI
LNKPILFYTY DLKLYQQKRG LVDNYLSIIP GRACYDSESL INEIQTPFNY SKIKVFSDRW
NKYSDGNSSQ NLLNFIENLI S
