TAGU_BACCZ
ID TAGU_BACCZ Reviewed; 303 AA.
AC Q630Y6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=BCE33L4961;
OS Bacillus cereus (strain ZK / E33L).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=288681;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZK / E33L;
RX PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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; CP000001; AAU15319.1; -; Genomic_DNA.
DR RefSeq; WP_000727088.1; NZ_CP009968.1.
DR AlphaFoldDB; Q630Y6; -.
DR SMR; Q630Y6; -.
DR EnsemblBacteria; AAU15319; AAU15319; BCE33L4961.
DR KEGG; bcz:BCE33L4961; -.
DR PATRIC; fig|288681.22.peg.388; -.
DR OMA; QMKINAA; -.
DR Proteomes; UP000002612; 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_1000065432"
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; 33743 MW; 183E17C1EC169605 CRC64;
MKKKILFWVL GILGVLIIGG GIYAYNVYSS VSNTLKEVHQ PLKRDQNNSN VGEKVSKSEP
VSILLLGADE RGEDKGRSDS LMVITLNPKN NSMKTVSIPR DTYTEIVGKG KSDKINHAYA
FGGVDMSVAT VENFLNVPIN YYIEVNMEGF KDIVDAVGGV DVKNDLEFTQ DGHHFAKGNI
HLTGDQALAF TRMRKQDPRG DFGRQMRQRQ VMQGVIKKGA SFSSLTGYGD VLAAIQKNVK
TNLTQDQMFD MQKNYKDCLK NSEDIQIPGD GHKAADGIWY YYVPDAAKQD LTNKLRTHLE
VTK