TARL_STAA8
ID TARL_STAA8 Reviewed; 562 AA.
AC Q2G1B8;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Teichoic acid ribitol-phosphate polymerase TarL {ECO:0000305};
DE EC=2.7.8.14 {ECO:0000269|PubMed:18215769, ECO:0000269|PubMed:18556787, ECO:0000269|PubMed:21035733};
DE AltName: Full=Poly(ribitol phosphate) polymerase TarL {ECO:0000305};
DE AltName: Full=Ribitol-phosphate polymerase TarL {ECO:0000303|PubMed:18556787};
DE AltName: Full=Tar polymerase TarL {ECO:0000305};
GN Name=tarL; OrderedLocusNames=SAOUHSC_00227 {ECO:0000312|EMBL:ABD29402.1};
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, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=NCTC 8325 / PS 47;
RX PubMed=18215769; DOI=10.1016/j.chembiol.2007.11.011;
RA Brown S., Zhang Y.H., Walker S.;
RT "A revised pathway proposed for Staphylococcus aureus wall teichoic acid
RT biosynthesis based on in vitro reconstitution of the intracellular steps.";
RL Chem. Biol. 15:12-21(2008).
RN [3]
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 [4]
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: 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 second glycerol phosphate attached to the
CC disaccharide linkage unit. Synthesizes polymers of more than 40 ribitol
CC phosphate units in length. {ECO:0000269|PubMed:18215769,
CC ECO:0000269|PubMed:18556787, 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:18215769, ECO:0000269|PubMed:18556787,
CC ECO:0000269|PubMed:21035733};
CC -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC biosynthesis. {ECO:0000269|PubMed:18215769}.
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; ABD29402.1; -; Genomic_DNA.
DR RefSeq; WP_000240920.1; NZ_LS483365.1.
DR RefSeq; YP_498822.1; NC_007795.1.
DR AlphaFoldDB; Q2G1B8; -.
DR SMR; Q2G1B8; -.
DR STRING; 1280.SAXN108_0237; -.
DR EnsemblBacteria; ABD29402; ABD29402; SAOUHSC_00227.
DR GeneID; 3920302; -.
DR KEGG; sao:SAOUHSC_00227; -.
DR PATRIC; fig|93061.5.peg.208; -.
DR eggNOG; COG1887; Bacteria.
DR HOGENOM; CLU_029598_3_1_9; -.
DR OMA; HAHTEED; -.
DR BioCyc; MetaCyc:MON-19978; -.
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..562
FT /note="Teichoic acid ribitol-phosphate polymerase TarL"
FT /id="PRO_0000438796"
SQ SEQUENCE 562 AA; 66075 MW; F2FD62222EFFD97B CRC64;
MVKSKIYIDK IYWERVQLFV EGHSENLDLE DSNFVLRNLT ETRTMKANDV KIDGNQFVCR
FNVAILDNGY YLPEDKYLLV NEQELDYIAQ LNPDVINDAY QNLKPEQEEE YNELETQNGK
INFLLQTYLK EFRKGGISKK TVYTVTPEIS SDVNEFVLDV VVTTPEVKSI YIVRKYKELR
KYFRKQSFNT RQFIFKAIFN TTKFFHLKKG NTVLFTSDSR PTMSGNFEYI YNEMLRQNLD
KKYDIHTVFK ANITDRRGII DKFRLPYLLG KADYIFVDDF HPLIYTVRFR RSQEVIQVWH
AVGAFKTVGF SRTGKKGGPF IDSLNHRSYT KAYVSSETDI PFYAEAFGIK EKNVVPTGVP
RTDVLFDEAY ATQIKQEMED ELPIIKGKKV ILFAPTFRGS GHGTAHYPFF KIDFERLARY
CEKNNAVVLF KMHPFVKNRL NIADKHKQYF VDVSDFREVN DILFITDLLI SDYSSLIYEY
AVFKKPMIFY AFDLEDYITT RDFYEPYESF VPGKIVQSFD ALMDALDNED YEGEKVIPFL
DKHFKYQDGR SSERLVRNLF GS
