TAGU_OCEIH
ID TAGU_OCEIH Reviewed; 320 AA.
AC Q8ENF3;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 103.
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=OB2530;
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC14486.1; -; Genomic_DNA.
DR RefSeq; WP_011066923.1; NC_004193.1.
DR AlphaFoldDB; Q8ENF3; -.
DR SMR; Q8ENF3; -.
DR STRING; 221109.22778216; -.
DR EnsemblBacteria; BAC14486; BAC14486; BAC14486.
DR KEGG; oih:OB2530; -.
DR eggNOG; COG1316; Bacteria.
DR HOGENOM; CLU_016455_2_2_9; -.
DR OMA; LLGYKDC; -.
DR OrthoDB; 491753at2; -.
DR PhylomeDB; Q8ENF3; -.
DR Proteomes; UP000000822; 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..320
FT /note="Polyisoprenyl-teichoic acid--peptidoglycan teichoic
FT acid transferase TagU"
FT /id="PRO_0000218500"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01140"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01140"
FT TOPO_DOM 37..320
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01140"
SQ SEQUENCE 320 AA; 35778 MW; 64BF1BBC6452AF14 CRC64;
MVSRTERKQH KKRRKWPFWL GGILLVLLLL ISGGIFLIYN QVGAVVDTMH SPLSRDSDPD
RQKEINQLYK EKDAVNILLL GVDERDGDLG RSDTMILLSI NPNTDKMIML SIPRDTYVNI
PGRGMDKINH AYPFGIVDGV GGPDLSVQTV EETFNLSIHS YIRVNMEGFQ QGIDAVGGVT
VNNAQAFSTG GYNFDQGQIT LDGKQALEFI RMRKQDSRGD LGRNDRQRQV IQAAMNEAAS
FSSITKAGEI LDILGNNVQT DLDMDKLQTL LTNYAGARNN ITTMEIEGHG ETINGIWYYI
VSDEEINRVN SEITGHMQEQ