TARL_BACSH
ID TARL_BACSH Reviewed; 619 AA.
AC Q8RKJ2; B7ZDK4; E0U4Y0;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Teichoic acid poly(ribitol-phosphate) polymerase {ECO:0000305};
DE EC=2.7.8.47 {ECO:0000269|PubMed:21035733};
DE AltName: Full=Poly(ribitol phosphate) polymerase;
DE AltName: Full=Tar polymerase;
GN Name=tarL; OrderedLocusNames=BSUW23_17580;
OS Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) (Bacillus
OS subtilis subsp. spizizenii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=655816;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX PubMed=11882717; DOI=10.1099/00221287-148-3-815;
RA Lazarevic V., Abellan F.-X., Beggah Moeller S., Karamata D., Maueel C.;
RT "Comparison of ribitol and glycerol teichoic acid genes in Bacillus
RT subtilis W23 and 168: identical function, similar divergent organization,
RT but different regulation.";
RL Microbiology 148:815-824(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RA Soldo B., Freymond P.P., Karamata D., Lazarevic V.;
RT "Minor teichoic acid of Bacillus subtilis W23.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX PubMed=21527469; DOI=10.1099/mic.0.048520-0;
RA Zeigler D.R.;
RT "The genome sequence of Bacillus subtilis subsp. spizizenii W23: insights
RT into speciation within the B. subtilis complex and into the history of B.
RT subtilis genetics.";
RL Microbiology 157:2033-2041(2011).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX PubMed=21035733; DOI=10.1016/j.chembiol.2010.07.017;
RA Brown S., Meredith T., Swoboda J., Walker S.;
RT "Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall
RT teichoic acids using different enzymatic pathways.";
RL Chem. Biol. 17:1101-1110(2010).
RN [5]
RP REVIEW.
RX PubMed=24024634; DOI=10.1146/annurev-micro-092412-155620;
RA Brown S., Santa Maria J.P. Jr., Walker S.;
RT "Wall teichoic acids of gram-positive bacteria.";
RL Annu. Rev. Microbiol. 67:313-336(2013).
CC -!- FUNCTION: Responsible for the polymerization of the main chain of the
CC major teichoic acid by sequential transfer of ribitol phosphate units
CC from CDP-ribitol to the glycerol phosphate attached to the disaccharide
CC linkage unit. Synthesizes polymers of up to 40 ribitol phosphate units
CC in length. {ECO:0000269|PubMed:21035733}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-O-[1-D-ribitylphospho-(2R)-1-glycerylphospho]-N-acetyl-beta-
CC D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-
CC cis-undecaprenyl diphosphate + n CDP-L-ribitol = 4-O-[(D-
CC ribitylphospho)(n)-D-ribitylphospho-(2R)-glycerylphospho]-N-acetyl-
CC beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-
CC trans,octa-cis-undecaprenyl diphosphate + n CMP + n H(+);
CC Xref=Rhea:RHEA:44668, Rhea:RHEA-COMP:12833, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57608, ChEBI:CHEBI:60377, ChEBI:CHEBI:133892,
CC ChEBI:CHEBI:133894; EC=2.7.8.47;
CC Evidence={ECO:0000269|PubMed:21035733};
CC -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC biosynthesis. {ECO:0000269|PubMed:21035733}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CDP-glycerol glycerophosphotransferase
CC family. {ECO:0000305}.
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DR EMBL; AJ313428; CAC86106.1; -; Genomic_DNA.
DR EMBL; AM260209; CAJ97393.1; -; Genomic_DNA.
DR EMBL; CP002183; ADM39551.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8RKJ2; -.
DR SMR; Q8RKJ2; -.
DR EnsemblBacteria; ADM39551; ADM39551; BSUW23_17580.
DR KEGG; bss:BSUW23_17580; -.
DR HOGENOM; CLU_029598_3_1_9; -.
DR OMA; VCFEYAL; -.
DR BioCyc; MetaCyc:MON-19965; -.
DR BRENDA; 2.7.8.47; 658.
DR UniPathway; UPA00790; -.
DR Proteomes; UP000002233; 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 Teichoic acid biosynthesis; Transferase.
FT CHAIN 1..619
FT /note="Teichoic acid poly(ribitol-phosphate) polymerase"
FT /id="PRO_0000208451"
SQ SEQUENCE 619 AA; 72598 MW; FBE2FBE1F6F8B770 CRC64;
MKLARKIKNR LFRSKKKTQK ENTAVIVHPA DNRVFSLFDK TKRIEENQQV PVRKISEFSW
NGSILKIAGY MYIKGLPLQK EDQVRKRLLL VNNGVLFTAV SLRDIPVDQL SIDTSNVPGA
YKWAGFSQQI NFSKLMNDKP LPQGEYKLFL EIEAVDDQNV KHQEVHTVGN VSNFLSNDVY
ATKMEFHSAK KLMKFNLIVN YDEGEKTINL SCNKLQEIDP SLLELDTGKE ANRFIRKLNT
SLFHFAYDVF RLLPIKSNKI VFASDSRLDV TGNFEFVYEE LLKREENFDF KFFLKSSIRD
RKSLSELMSM AYHFATSKII FIDDFYPIIY PLKIRKNADL VQLWHAVGAF KTFGYSRIGL
PGGPSPHSKN HRNYTKVIVS SENIRKHYAE GFGVDIENVI ATGVPRTDFF FDEAKKAFVK
ERLYTEYPFL KDKKVILFAP TFRGNGQQSA HYPFEVLDFD RLYRELKDEY IFLFKIHPFV
RNDANIPYQY SDFFYDFSSF REINELLLVT DVLITDYSSV CFEYALLNKP MIFFSYDVDD
YIRKRDFYYD YFDFIPGPLA KTSDQMISII KEEKYNFEQI DSFVHYFFDD LDGKASERVV
DQIVFPQEEE PVDDKVLKR
