ID   TAGU_BACC0              Reviewed;         303 AA.
AC   B7JGI9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 66.
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};
GN   OrderedLocusNames=BCAH820_5355;
OS   Bacillus cereus (strain AH820).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405535;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH820;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH820.";
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; CP001283; ACK89455.1; -; Genomic_DNA.
DR   RefSeq; WP_000727086.1; NC_011773.1.
DR   AlphaFoldDB; B7JGI9; -.
DR   SMR; B7JGI9; -.
DR   EnsemblBacteria; ACK89455; ACK89455; BCAH820_5355.
DR   KEGG; bcu:BCAH820_5355; -.
DR   HOGENOM; CLU_016455_2_2_9; -.
DR   OMA; QMKINAA; -.
DR   Proteomes; UP000001363; 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; 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_1000137341"
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;  33703 MW;  759E994F3014A7ED CRC64;
     MKKKILFWVL GILGVLIIGG GIYAYNVYSS VSNTLKEVHQ PLKRDQNNSN VGEKVSKSEP
     VSILLLGADE RGDDKGRSDS LMVITLNPKN NSMKTVSIPR DTYTEIVGKG KSDKINHAYA
     FGGVDMSVAT VEKFLDVPIN YYIEVNMEGF KDIVDAVGGV DVTNDLEFTQ DGHHFAKGNI
     HLTGDQALAF TRMRKQDPRG DFGRQMRQRQ VMQGVIKKGA SFSSLTGYGD VLAAIQKNVK
     TNLTQDQMFD MQKNYKDCLK NSEDIQIPGD GHKAADGIWY YYVPDAAKQD LTNKLRSHLE
     VTK