ID   TAGU_BACMK              Reviewed;         304 AA.
AC   A9VRA8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=BcerKBAB4_5058;
OS   Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000903; ABY46204.1; -; Genomic_DNA.
DR   RefSeq; WP_012262019.1; NC_010184.1.
DR   AlphaFoldDB; A9VRA8; -.
DR   SMR; A9VRA8; -.
DR   STRING; 315730.BcerKBAB4_5058; -.
DR   EnsemblBacteria; ABY46204; ABY46204; BcerKBAB4_5058.
DR   KEGG; bwe:BcerKBAB4_5058; -.
DR   eggNOG; COG1316; Bacteria.
DR   HOGENOM; CLU_016455_2_2_9; -.
DR   OMA; GYIMINM; -.
DR   Proteomes; UP000002154; 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..304
FT                   /note="Polyisoprenyl-teichoic acid--peptidoglycan teichoic
FT                   acid transferase TagU"
FT                   /id="PRO_1000137342"
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..304
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01140"
SQ   SEQUENCE   304 AA;  33809 MW;  64D2182FE74E5DC4 CRC64;
     MKKKILFWIL GIIGIMIIGG GVYAYNVYSS VSKTLDEVHK PLKRDKDSNG VETAKISKSE
     PVSILLLGAD ERGEDKGRSD SLMVITLNPK NNSMKTVSIP RDTYTEIVGK GKSDKINHAY
     AFGGVDMSVA TVEKFLSVPI NYYIEVNMEG FKDIVDAVGG VDVNNDLEFT ANGHHFAKGN
     VHLTGDQALA FTRMRKEDPR GDFGRQMRQR QVMQAVIKKG ASFSSLSSYG DVLTAIQKNV
     KTNLTQDQMF DMQKNYKNCL QNSEEIQIPG DGHKAADGIW YYYVPDAAKQ DITNKLRAHL
     ELTK