TAGF_STAEQ
ID TAGF_STAEQ Reviewed; 721 AA.
AC Q5HLM5;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Teichoic acid poly(glycerol phosphate) polymerase {ECO:0000305};
DE EC=2.7.8.12 {ECO:0000269|PubMed:20400947};
DE AltName: Full=CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase {ECO:0000305};
DE AltName: Full=CGPTase {ECO:0000305};
DE AltName: Full=Major teichoic acid biosynthesis protein F {ECO:0000305};
DE AltName: Full=Poly(glycerol phosphate) polymerase {ECO:0000305};
DE AltName: Full=Tag polymerase {ECO:0000305};
GN Name=tagF {ECO:0000312|EMBL:AAW52851.1};
GN OrderedLocusNames=SERP1960 {ECO:0000312|EMBL:AAW52851.1};
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A {ECO:0000312|Proteomes:UP000000531};
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 313-721 OF APOENZYME; MUTANT
RP ALA-584 AND OF MUTANT ASN-444 IN COMPLEX WITH GLYCEROL-CDP, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=20400947; DOI=10.1038/nsmb.1819;
RA Lovering A.L., Lin L.Y., Sewell E.W., Spreter T., Brown E.D.,
RA Strynadka N.C.;
RT "Structure of the bacterial teichoic acid polymerase TagF provides insights
RT into membrane association and catalysis.";
RL Nat. Struct. Mol. Biol. 17:582-589(2010).
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:20400947}.
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:20400947};
CC -!- PATHWAY: Cell wall biogenesis; poly(glycerol 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000029; AAW52851.1; -; Genomic_DNA.
DR PDB; 3L7I; X-ray; 2.70 A; A/B/C/D=1-721.
DR PDB; 3L7J; X-ray; 2.81 A; A/B/C/D=1-721.
DR PDB; 3L7K; X-ray; 3.10 A; A/B/C/D=1-721.
DR PDB; 3L7L; X-ray; 2.95 A; A/B/C/D=1-721.
DR PDB; 3L7M; X-ray; 2.85 A; A/B/C/D=1-721.
DR PDBsum; 3L7I; -.
DR PDBsum; 3L7J; -.
DR PDBsum; 3L7K; -.
DR PDBsum; 3L7L; -.
DR PDBsum; 3L7M; -.
DR AlphaFoldDB; Q5HLM5; -.
DR SMR; Q5HLM5; -.
DR STRING; 176279.SERP1960; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblBacteria; AAW52851; AAW52851; SERP1960.
DR KEGG; ser:SERP1960; -.
DR eggNOG; COG0463; Bacteria.
DR eggNOG; COG1887; Bacteria.
DR HOGENOM; CLU_003394_2_0_9; -.
DR OMA; DCSPDAC; -.
DR BRENDA; 2.7.8.12; 5875.
DR UniPathway; UPA00827; -.
DR EvolutionaryTrace; Q5HLM5; -.
DR Proteomes; UP000000531; 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 Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR007554; Glycerophosphate_synth.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR043148; TagF_C.
DR InterPro; IPR043149; TagF_N.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF04464; Glyphos_transf; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell wall biogenesis/degradation; Membrane;
KW Reference proteome; Teichoic acid biosynthesis; Transferase.
FT CHAIN 1..721
FT /note="Teichoic acid poly(glycerol phosphate) polymerase"
FT /id="PRO_0000438782"
FT BINDING 443..447
FT /ligand="CDP-glycerol"
FT /ligand_id="ChEBI:CHEBI:58311"
FT /evidence="ECO:0000269|PubMed:20400947,
FT ECO:0007744|PDB:3L7K, ECO:0007744|PDB:3L7L"
FT BINDING 511
FT /ligand="CDP-glycerol"
FT /ligand_id="ChEBI:CHEBI:58311"
FT /evidence="ECO:0000269|PubMed:20400947,
FT ECO:0007744|PDB:3L7K, ECO:0007744|PDB:3L7L"
FT BINDING 545..546
FT /ligand="CDP-glycerol"
FT /ligand_id="ChEBI:CHEBI:58311"
FT /evidence="ECO:0000269|PubMed:20400947,
FT ECO:0007744|PDB:3L7K, ECO:0007744|PDB:3L7L"
FT BINDING 582..584
FT /ligand="CDP-glycerol"
FT /ligand_id="ChEBI:CHEBI:58311"
FT /evidence="ECO:0000269|PubMed:20400947,
FT ECO:0007744|PDB:3L7K, ECO:0007744|PDB:3L7L"
FT BINDING 624..625
FT /ligand="CDP-glycerol"
FT /ligand_id="ChEBI:CHEBI:58311"
FT /evidence="ECO:0000269|PubMed:20400947,
FT ECO:0007744|PDB:3L7K, ECO:0007744|PDB:3L7L"
FT BINDING 629
FT /ligand="CDP-glycerol"
FT /ligand_id="ChEBI:CHEBI:58311"
FT /evidence="ECO:0000269|PubMed:20400947,
FT ECO:0007744|PDB:3L7K, ECO:0007744|PDB:3L7L"
FT HELIX 316..331
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 336..344
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:3L7I"
FT STRAND 351..359
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 367..379
FT /evidence="ECO:0007829|PDB:3L7I"
FT STRAND 383..391
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:3L7I"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 409..417
FT /evidence="ECO:0007829|PDB:3L7I"
FT STRAND 418..425
FT /evidence="ECO:0007829|PDB:3L7I"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:3L7K"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 452..454
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 465..476
FT /evidence="ECO:0007829|PDB:3L7I"
FT STRAND 480..486
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 487..496
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:3L7I"
FT STRAND 504..507
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 510..512
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 513..517
FT /evidence="ECO:0007829|PDB:3L7I"
FT TURN 518..520
FT /evidence="ECO:0007829|PDB:3L7J"
FT HELIX 522..531
FT /evidence="ECO:0007829|PDB:3L7I"
FT STRAND 539..543
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 549..551
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 554..556
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 566..573
FT /evidence="ECO:0007829|PDB:3L7I"
FT TURN 574..576
FT /evidence="ECO:0007829|PDB:3L7I"
FT STRAND 577..581
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 585..588
FT /evidence="ECO:0007829|PDB:3L7I"
FT TURN 597..599
FT /evidence="ECO:0007829|PDB:3L7I"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 609..614
FT /evidence="ECO:0007829|PDB:3L7I"
FT STRAND 617..623
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 626..630
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 631..633
FT /evidence="ECO:0007829|PDB:3L7I"
FT STRAND 637..640
FT /evidence="ECO:0007829|PDB:3L7I"
FT TURN 642..648
FT /evidence="ECO:0007829|PDB:3L7I"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:3L7I"
FT STRAND 660..664
FT /evidence="ECO:0007829|PDB:3L7I"
FT STRAND 666..669
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 670..677
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 680..686
FT /evidence="ECO:0007829|PDB:3L7I"
FT HELIX 688..698
FT /evidence="ECO:0007829|PDB:3L7I"
FT TURN 699..701
FT /evidence="ECO:0007829|PDB:3L7J"
FT HELIX 706..721
FT /evidence="ECO:0007829|PDB:3L7I"
SQ SEQUENCE 721 AA; 85851 MW; 9B9EE6AEE5EA472B CRC64;
MNKLTIIVTY YNAEEYITGC LESIKQQRTQ DFNLIIVNDG STDQSKKLMD EAIKDYDKNI
RFIDLDENSG HAHARNIALE EVETPYFMFL DADDELASYA ITFYLEKFNN TDGLIAPIHS
FTTQRPQFVD LDRVRVEYFN AKENINSFLR KQSACNIIFR TAIVRAHHIR FNENLNTYVD
WSFVLEYMKY VNKFVRIFNF PFYFRGEVYD PFETLTLSEQ NFDILFKDYV NSFYDAIKRA
TNPKVREFIV TKMGNKIANE FEPTRYDINE RYQTHKDTLV ELSKFLHVHL VKNQKLINKI
ETILLMNNET DKAFKVNQFR KTLRHVKNIV LRRKNKERSL YDLTDKEDNV KPKTIVFESF
GGKNYSDSPK YIYEYMQKYY PNYRYIWSFK NPDKNVVPGS AEKVKRNSAE YYQAYSEASH
WVSNARTPLY LNKKENQTYI QTWHGTPLKR LANDMKVVRM PGTTTPKYKR NFNRETSRWD
YLISPNRYST EIFRSAFWMD EERILEIGYP RNDVLVNRAN DQEYLDEIRT HLNLPSDKKV
IMYAPTWRDD EFVSKGKYLF ELKIDLDNLY KELGDDYVIL LRMHYLISNA LDLSGYENFA
IDVSNYNDVS ELFLISDCLI TDYSSVMFDY GILKRPQFFF AYDIDKYDKG LRGFYMNYME
DLPGPIYTEP YGLAKELKNL DKVQQQYQEK IDAFYDRFCS VDNGKASQYI GDLIHKDIKE
Q
