ID   TAGU_BACAC              Reviewed;         303 AA.
AC   C3LEN7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=BAMEG_5552;
OS   Bacillus anthracis (strain CDC 684 / NRRL 3495).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=568206;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 684 / NRRL 3495;
RA   Dodson R.J., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., Han C.,
RA   Sutton G., Sims D.;
RT   "Genome sequence of Bacillus anthracis str. CDC 684.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001215; ACP14988.1; -; Genomic_DNA.
DR   RefSeq; WP_000727089.1; NC_012581.1.
DR   AlphaFoldDB; C3LEN7; -.
DR   SMR; C3LEN7; -.
DR   GeneID; 45025096; -.
DR   KEGG; bah:BAMEG_5552; -.
DR   HOGENOM; CLU_016455_2_2_9; -.
DR   OMA; QMKINAA; -.
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; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..303
FT                   /note="Polyisoprenyl-teichoic acid--peptidoglycan teichoic
FT                   acid transferase TagU"
FT                   /id="PRO_1000164095"
FT   TOPO_DOM        1..4
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01140"
FT   TRANSMEM        5..25
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01140"
FT   TOPO_DOM        26..303
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01140"
SQ   SEQUENCE   303 AA;  33759 MW;  4228DB1BEC168E7D CRC64;
     MKKKILFWVL GILGVLIIGG GIYAYNVYSS VSNTLKEVHQ PLKRDQNNSN VGEKVSKSEP
     VSILLLGADE RGEDKGRSDS LMVITLNPKN NSMKTVSIPR DTYTEIVGKG KSDKINHAYA
     FGGVDMSVAT VENFLNVPIN YYIEVNMEGF KDIVDAVGGV DVKNDLEFTQ DGHHFAKGNI
     HLTGDQALAF TRMRKQDPRG DFGRQMRQRQ VMQGVIKKGA SFSSLTGYGD VLSAIQKNVK
     TNLTQDQMFD MQKNYKDCLK NSEDIQIPGD GHKAADGIWY YYVPDAAKQD LTNKLRTHLE
     VTK