TAGU_BACCR
ID TAGU_BACCR Reviewed; 304 AA.
AC Q815A2;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=BC_5265;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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; AE016877; AAP12129.1; -; Genomic_DNA.
DR RefSeq; NP_834928.1; NC_004722.1.
DR RefSeq; WP_000727039.1; NZ_CP034551.1.
DR AlphaFoldDB; Q815A2; -.
DR SMR; Q815A2; -.
DR STRING; 226900.BC_5265; -.
DR EnsemblBacteria; AAP12129; AAP12129; BC_5265.
DR KEGG; bce:BC5265; -.
DR PATRIC; fig|226900.8.peg.5435; -.
DR HOGENOM; CLU_016455_2_2_9; -.
DR OMA; THAYVYG; -.
DR Proteomes; UP000001417; 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..304
FT /note="Polyisoprenyl-teichoic acid--peptidoglycan teichoic
FT acid transferase TagU"
FT /id="PRO_0000218496"
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; 34051 MW; 60463F9328A44542 CRC64;
MKKKILFWIL GIIGILIIGG GAYAYSIYSS VSKTLDEVHK PLKRDKDSKG TEEVKISKSE
PVSILLLGVD ERGNEKGRSD SLILITLNPK NNSMKTVSIP RDTYTEIVGK GKSDKINHAY
AFGGVDMSVA TVEKFLNVPI NYYIEVNMAG FKDIVDAVGG VDVNNDLEFK QDKHHFAKGN
IHLTGDEALS FTRMRYEDPR GDFGRQMRQR QVMQAVIKKG ATFSSLTSYG DVLTAIQKNV
KTNLTQDQMF DMQKNYKNCL ENSEDIQIPG DGHKAADGIW YYYVPEAAKQ DLTNKLRAHL
EVTK