TAGU_ALKHC
ID TAGU_ALKHC Reviewed; 304 AA.
AC Q9K6Q8;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-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=BH3670;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB07389.1; -; Genomic_DNA.
DR PIR; F84108; F84108.
DR RefSeq; WP_010899796.1; NC_002570.2.
DR AlphaFoldDB; Q9K6Q8; -.
DR SMR; Q9K6Q8; -.
DR STRING; 272558.10176294; -.
DR EnsemblBacteria; BAB07389; BAB07389; BAB07389.
DR KEGG; bha:BH3670; -.
DR eggNOG; COG1316; Bacteria.
DR HOGENOM; CLU_016455_2_2_9; -.
DR OMA; LLGYKDC; -.
DR OrthoDB; 491753at2; -.
DR Proteomes; UP000001258; 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_0000218497"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01140"
FT TRANSMEM 4..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01140"
FT TOPO_DOM 25..304
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01140"
SQ SEQUENCE 304 AA; 33590 MW; CF1F0C66330E3952 CRC64;
MKKALIAIGL ILGTITVAII GYGIYLYSSI QNTAGEMHEP LDRGDKSDKR DVAFDISAQD
PFSILIAGVD SREDTHAGRS DTLIVLTVNP KEESIKMLSI PRDTRTEIVG RGTDDKINHA
YAFGGAQMTI DTVENFLDIP IDHYVSINMD GFTQLVDALG GVSVENSFAF SQNGYQFEEG
EIFLETGDEA LAYARMRKQD SRGDFGRNDR QRQIVEAVIK QSAQFSSITK AGAILDAVGE
SVRTDLQLDG MWELQSNYRG AAKNIEQLEI TGEGTRINNI YYLIIPQEEI ARVQGELKSH
LELS
