ID   TAGU_BACLD              Reviewed;         306 AA.
AC   Q65E87; Q62PQ7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=BLi03811, BL02430;
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA   Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT   with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
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; CP000002; AAU25254.1; -; Genomic_DNA.
DR   EMBL; AE017333; AAU42627.1; -; Genomic_DNA.
DR   RefSeq; WP_011198358.1; NC_006322.1.
DR   AlphaFoldDB; Q65E87; -.
DR   SMR; Q65E87; -.
DR   STRING; 279010.BL02430; -.
DR   PRIDE; Q65E87; -.
DR   DNASU; 3101012; -.
DR   EnsemblBacteria; AAU25254; AAU25254; BL02430.
DR   KEGG; bld:BLi03811; -.
DR   KEGG; bli:BL02430; -.
DR   PATRIC; fig|279010.13.peg.3877; -.
DR   eggNOG; COG1316; Bacteria.
DR   HOGENOM; CLU_016455_2_2_9; -.
DR   OMA; QMKINAA; -.
DR   OrthoDB; 491753at2; -.
DR   BioCyc; BLIC279010:BLI_RS18740-MON; -.
DR   Proteomes; UP000000606; 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..306
FT                   /note="Polyisoprenyl-teichoic acid--peptidoglycan teichoic
FT                   acid transferase TagU"
FT                   /id="PRO_1000065433"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01140"
FT   TRANSMEM        12..32
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01140"
FT   TOPO_DOM        33..306
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01140"
SQ   SEQUENCE   306 AA;  34553 MW;  DD43306AF55BBD59 CRC64;
     MRAEKRKKKK KILYTIIALI GIFVLSTGSY AYYLWHKAAS TVANIHENIN KSKKRDSAVD
     IDNHDPFSVL LMGVDERDGD KGRADSLIYM TVNPKTKTTE MVSIPRDTYT EIIGKGKMDK
     INHSYAFGGV QMTVDTVENF LDVPVDYFIK VNMESFKDVV DTLGGITVNS TFAFNYDGYS
     FGKGEITLNG KEALAYTRMR KEDPNGDFGR QNRQRQVIEG IINKGANISS ITKFGDMFKV
     IENNVKTNLT FDDMWDIQSG YKEARSKVIQ HELKGDGTKI NGIYYYKADE SSLSDITAEL
     KESLNK