ID A0A1H3T917_9BACI Unreviewed; 312 AA.
AC A0A1H3T917;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN05421736_113109 {ECO:0000313|EMBL:SDZ46447.1};
OS Evansella caseinilytica.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Evansella.
OX NCBI_TaxID=1503961 {ECO:0000313|EMBL:SDZ46447.1, ECO:0000313|Proteomes:UP000198935};
RN [1] {ECO:0000313|Proteomes:UP000198935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP {ECO:0000313|Proteomes:UP000198935};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNPI01000013; SDZ46447.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3T917; -.
DR STRING; 1503961.SAMN05421736_113109; -.
DR OrthoDB; 27330at2; -.
DR Proteomes; UP000198935; Unassembled WGS sequence.
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:UP000198935};
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..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01140"
FT TOPO_DOM 25..312
FT /note="Extracellular"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01140"
FT DOMAIN 77..218
FT /note="Cell envelope-related transcriptional attenuator"
FT /evidence="ECO:0000259|Pfam:PF03816"
SQ SEQUENCE 312 AA; 34697 MW; 7BB9AC3C81DE5DA3 CRC64;
MKKVLLIIGL SVLTVGLAIG GYGFYIYKSM QSAVDSMHQP IDRTKSDKRE VAVDIDSQEP
LAFLLMGVDE RGADKGRTDT IIVITVNPEE ESMKMVSIPR DTYTEIVGRG TMDKINHAYA
FGGPEMAINT VENFFDIPLD YFVTINMEGF KEIVDVLGGV SVESEMAFSY GGYDFDEGIL
ELDGEAALAY SRMRYEDPRG DLGRNDRQRQ IIDAIIKEGA QFSTITKADD ILDSLGKNVA
TNLTFDEMMK IQSNYAKARH NSETLEFSGN GGGKKDGIWY LFVPEEEREH VSHELRVHLG
IEDSSEVAAA EE
//
