ID A0A223KV88_9BACI Unreviewed; 311 AA.
AC A0A223KV88;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Polyisoprenyl-teichoic acid--peptidoglycan teichoic acid transferase TagU {ECO:0000256|HAMAP-Rule:MF_01140};
DE EC=2.7.8.- {ECO:0000256|HAMAP-Rule:MF_01140};
GN Name=tagU {ECO:0000256|HAMAP-Rule:MF_01140};
GN ORFNames=BC6307_20035 {ECO:0000313|EMBL:AST93389.1};
OS Sutcliffiella cohnii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Sutcliffiella.
OX NCBI_TaxID=33932 {ECO:0000313|EMBL:AST93389.1, ECO:0000313|Proteomes:UP000215224};
RN [1] {ECO:0000313|EMBL:AST93389.1, ECO:0000313|Proteomes:UP000215224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6307 {ECO:0000313|EMBL:AST93389.1,
RC ECO:0000313|Proteomes:UP000215224};
RA Lee Y.-J., Yi H., Bahn Y.-S., Kim J.F., Lee D.-W.;
RT "The whole genome sequencing and assembly of Bacillus cohnii DSM 6307T
RT strain.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01140}.
CC -!- PATHWAY: Cell wall biogenesis. {ECO:0000256|HAMAP-Rule:MF_01140}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01140};
CC Single-pass type II membrane protein {ECO:0000256|HAMAP-Rule:MF_01140}.
CC -!- SIMILARITY: Belongs to the LytR/CpsA/Psr (LCP) family.
CC {ECO:0000256|ARBA:ARBA00006068, ECO:0000256|HAMAP-Rule:MF_01140}.
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DR EMBL; CP018866; AST93389.1; -; Genomic_DNA.
DR RefSeq; WP_066420871.1; NZ_CP018866.1.
DR AlphaFoldDB; A0A223KV88; -.
DR STRING; 1314751.GCA_001591425_04526; -.
DR KEGG; bcoh:BC6307_20035; -.
DR Proteomes; UP000215224; Chromosome.
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 Gene3D; 3.40.630.190; LCP protein; 1.
DR HAMAP; MF_01140; TagU_transferase; 1.
DR InterPro; IPR004474; LytR_CpsA_psr.
DR InterPro; IPR023734; TagU.
DR NCBIfam; TIGR00350; lytR_cpsA_psr; 1.
DR PANTHER; PTHR33392; POLYISOPRENYL-TEICHOIC ACID--PEPTIDOGLYCAN TEICHOIC ACID TRANSFERASE TAGU; 1.
DR PANTHER; PTHR33392:SF6; POLYISOPRENYL-TEICHOIC ACID--PEPTIDOGLYCAN TEICHOIC ACID TRANSFERASE TAGU; 1.
DR Pfam; PF03816; LytR_cpsA_psr; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01140};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_01140};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01140};
KW Reference proteome {ECO:0000313|Proteomes:UP000215224};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968, ECO:0000256|HAMAP-
KW Rule:MF_01140};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01140};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01140};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01140}.
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01140"
FT TRANSMEM 14..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 32..311
FT /note="Extracellular"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01140"
FT DOMAIN 87..228
FT /note="Cell envelope-related transcriptional attenuator"
FT /evidence="ECO:0000259|Pfam:PF03816"
SQ SEQUENCE 311 AA; 35023 MW; 5412CC4D9ABA3F1E CRC64;
MRKKLKNLKK WQKYTFLIIG VLFLVVGSMV GYAFYNVNKT LSTMHQPIER EHSDKRPEKV
NFIEQDPISI LLIGVDSRNG NLERGLSDTL MVITVNPDDK SMKMVSIPRD TRTEIVGKGF
EDKINHAHSF GGVEMAIPTV ENFLDIPIDY YVKINMEGFK DLVDAVGGVE VNNSFAFSTG
GMDFPEGKIS LNGKEALAFS RMRKQDPRGD FGRTDRQKQI VQAVIKKGAS FSGITNLDSI
LNAIGQNVKT DIASTEMLDI QKNYKEAIND LEVLQITGTG TTISRIYYLQ VPEEERLRIS
TILKEHLKLN E
//
