TARK_STAA8
ID TARK_STAA8 Reviewed; 513 AA.
AC Q2G1C2;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Teichoic acid ribitol-phosphate polymerase TarK {ECO:0000305};
DE EC=2.7.8.14 {ECO:0000269|PubMed:18556787, ECO:0000269|PubMed:21035733};
DE AltName: Full=Poly(ribitol phosphate) polymerase TarK {ECO:0000305};
DE AltName: Full=Ribitol-phosphate polymerase TarK {ECO:0000305};
DE AltName: Full=Tar polymerase TarK {ECO:0000305};
GN Name=tarK; OrderedLocusNames=SAOUHSC_00222 {ECO:0000312|EMBL:ABD29398.1};
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47 {ECO:0000312|Proteomes:UP000008816};
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=RN4220 / SA178RI;
RX PubMed=18556787; DOI=10.1128/jb.00526-08;
RA Pereira M.P., D'Elia M.A., Troczynska J., Brown E.D.;
RT "Duplication of teichoic acid biosynthetic genes in Staphylococcus aureus
RT leads to functionally redundant poly(ribitol phosphate) polymerases.";
RL J. Bacteriol. 190:5642-5649(2008).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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).
CC -!- FUNCTION: Can catalyze 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 second glycerol phosphate attached to the
CC disaccharide linkage unit. {ECO:0000269|PubMed:18556787,
CC ECO:0000269|PubMed:21035733}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-O-[di(2R)-glycerylphospho]-N-acetyl-beta-D-mannosaminyl-
CC (1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl
CC diphosphate + n CDP-L-ribitol = 4-O-[(D-ribitylphospho)(n)-di{(2R)-
CC glycerylphospho}]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-
CC D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + n CMP + n
CC H(+); Xref=Rhea:RHEA:13353, Rhea:RHEA-COMP:12840, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57608, ChEBI:CHEBI:60377, ChEBI:CHEBI:133867,
CC ChEBI:CHEBI:133896; EC=2.7.8.14;
CC Evidence={ECO:0000269|PubMed:18556787, ECO:0000269|PubMed:21035733};
CC -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC biosynthesis. {ECO:0000305}.
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; CP000253; ABD29398.1; -; Genomic_DNA.
DR RefSeq; WP_011446981.1; NC_007795.1.
DR RefSeq; YP_498818.1; NC_007795.1.
DR AlphaFoldDB; Q2G1C2; -.
DR SMR; Q2G1C2; -.
DR STRING; 1280.SAXN108_0232; -.
DR EnsemblBacteria; ABD29398; ABD29398; SAOUHSC_00222.
DR GeneID; 3920298; -.
DR KEGG; sao:SAOUHSC_00222; -.
DR PATRIC; fig|93061.5.peg.204; -.
DR eggNOG; COG1887; Bacteria.
DR HOGENOM; CLU_029598_3_1_9; -.
DR OMA; VQVWHAV; -.
DR BRENDA; 2.7.8.46; 3352.
DR BRENDA; 2.7.8.47; 3352.
DR UniPathway; UPA00790; -.
DR Proteomes; UP000008816; 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:0047356; F:CDP-ribitol ribitolphosphotransferase 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..513
FT /note="Teichoic acid ribitol-phosphate polymerase TarK"
FT /id="PRO_0000438795"
SQ SEQUENCE 513 AA; 60183 MW; CE9F8256AC66FBCA CRC64;
MKIDGNTFIC RFNVAILDDG YYLPMDKYLF VYHDQLEYIG QLNPNIIDQA YAALNEEQIE
EYNELTTQNG KVNYLLAYDA KVFRKGGVSQ HTVYTITPEI ASDVNEFVFD IEITLPQEKS
GVIATSAHWL HKQGHKASFE SRSFLFKAIF NITKLLHIKR SKTILFTSDS RPNLSGNFKY
VYDELLRQKV DFDYDIKTVF KENITDRRKW RDKFRLPYLL GKADYIFVDD FHPLIYTVRF
RPSQEIIQVW HAVGAFKTVG FSRTGKKGGP FIDSLNHRSY TKAYVSSETD IPFYAEAFGI
REENVVPTGV PRTDVLFDEA YATQIKQEME DELPIIKGKK VILFAPTFRG NGHGTAHYPF
FKIDFERLAR YCEKHNAVVL FKMHPFVKNR LNISREHRQY FIDVSDHREV NDILFVTDLL
ISDYSSLIYE YAVFKKPMIF YAFDLEDYIT TRDFYEPFES FVPGKIVQSF DALMDALDNE
DYEVEKVVPF LDKHFKYQDG RSSERLVKDL FRR
