TAGU_ENTFA
ID TAGU_ENTFA Reviewed; 303 AA.
AC Q836A6;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Polyisoprenyl-teichoic acid--peptidoglycan teichoic acid transferase TagU {ECO:0000255|HAMAP-Rule:MF_01140};
DE EC=2.7.8.- {ECO:0000255|HAMAP-Rule:MF_01140};
GN Name=tagU {ECO:0000255|HAMAP-Rule:MF_01140}; OrderedLocusNames=EF_1212;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
CC -!- FUNCTION: May catalyze the final step in cell wall teichoic acid
CC biosynthesis, the transfer of the anionic cell wall polymers (APs) from
CC their lipid-linked precursor to the cell wall peptidoglycan (PG).
CC {ECO:0000255|HAMAP-Rule:MF_01140}.
CC -!- PATHWAY: Cell wall biogenesis. {ECO:0000255|HAMAP-Rule:MF_01140}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01140};
CC Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_01140}.
CC -!- SIMILARITY: Belongs to the LytR/CpsA/Psr (LCP) family.
CC {ECO:0000255|HAMAP-Rule:MF_01140}.
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DR EMBL; AE016830; AAO81009.1; -; Genomic_DNA.
DR RefSeq; NP_814939.1; NC_004668.1.
DR RefSeq; WP_002385983.1; NZ_KE136528.1.
DR AlphaFoldDB; Q836A6; -.
DR SMR; Q836A6; -.
DR STRING; 226185.EF_1212; -.
DR DNASU; 1200112; -.
DR EnsemblBacteria; AAO81009; AAO81009; EF_1212.
DR KEGG; efa:EF1212; -.
DR PATRIC; fig|226185.45.peg.2287; -.
DR eggNOG; COG1316; Bacteria.
DR HOGENOM; CLU_016455_2_2_9; -.
DR OMA; LLGYKDC; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:UniProtKB-UniRule.
DR GO; GO:0070726; P:cell wall assembly; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01140; TagU_transferase; 1.
DR InterPro; IPR004474; LytR_CpsA_psr.
DR InterPro; IPR023734; TagU.
DR Pfam; PF03816; LytR_cpsA_psr; 1.
DR TIGRFAMs; TIGR00350; lytR_cpsA_psr; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell wall biogenesis/degradation; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..303
FT /note="Polyisoprenyl-teichoic acid--peptidoglycan teichoic
FT acid transferase TagU"
FT /id="PRO_0000218499"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01140"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01140"
FT TOPO_DOM 28..303
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01140"
SQ SEQUENCE 303 AA; 33855 MW; 2F84E21D450A7DF0 CRC64;
MSKGKKIFAI IFGIILVLFL AVVGMGAKLY WDVSKSMDKT YETVERSKKS QVNLNNKEPF
SVLLLGIDTG DDGRVEQGRS DTTIVATVNP RDKQTTLVSL ARDTYVDIPG QGKQDKLNHA
YAFGGASLAM DTVENYLNIP INHYVSINMA GLKELVNAVG GIEVNNNLTF SQDGYDFTIG
KISLDGEQAL SYSRMRYEDP NGDYGRQERQ RKVIEGIVQK VLSLNSVSNY QEILTAVSDN
MKTDLSFDDM KKIALDYRSA FGKVKQDQLQ GTGFMQDGVS YQRVDEQELT RVQQELKNQL
NTK