ID W1SGR6_9BACI Unreviewed; 308 AA.
AC W1SGR6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=BAVI_11779 {ECO:0000313|EMBL:ETI68586.1};
OS Neobacillus vireti LMG 21834.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI68586.1, ECO:0000313|Proteomes:UP000018877};
RN [1] {ECO:0000313|EMBL:ETI68586.1, ECO:0000313|Proteomes:UP000018877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI68586.1,
RC ECO:0000313|Proteomes:UP000018877};
RX PubMed=24708037; DOI=10.1111/1462-2920.12478;
RA Mania D., Heylen K., van Spanning R.J., Frostegard A.;
RT "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti is a
RT potent source and sink for nitric and nitrous oxide under high nitrate
RT conditions.";
RL Environ. Microbiol. 16:3196-3210(2014).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETI68586.1}.
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DR EMBL; ALAN01000065; ETI68586.1; -; Genomic_DNA.
DR RefSeq; WP_024028543.1; NZ_ALAN01000065.1.
DR AlphaFoldDB; W1SGR6; -.
DR STRING; 220686.AA980_19025; -.
DR PATRIC; fig|1131730.3.peg.2456; -.
DR eggNOG; COG1316; Bacteria.
DR OrthoDB; 27330at2; -.
DR Proteomes; UP000018877; 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:UP000018877};
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 TOPO_DOM 32..308
FT /note="Extracellular"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01140"
FT DOMAIN 84..225
FT /note="Cell envelope-related transcriptional attenuator"
FT /evidence="ECO:0000259|Pfam:PF03816"
SQ SEQUENCE 308 AA; 35106 MW; F5AB1135A7D7F34D CRC64;
MRAQKKKSRK WLRVTGIILL VLLIAGGAYG YTVYHSFKKA VITMHQPLER EISVKREKPV
VFEKKDPFSV LMLGVDEREG DKGRSDTIIV LAVNPINNSV KMLSIPRDTR TEIIGKGKED
KINHAYAFGG VPMSMDTVEN FLDIPIDYYI QINMEGFKDI VNAVGGVKVQ NDLDFTENGF
HFAKGEISLN GEQALSFARM RYNDPRGDFG RQLRQRQIIQ AIINEGTSVS TLTKFSDIFT
ALGKNIKTNL TFDQIMDIQK NYRDAGKNIQ QMEINETGTM INKIYYGLVS EEEKQRIRTE
LKKQLELQ
//
