ID A0A0K9GW97_9BACI Unreviewed; 311 AA.
AC A0A0K9GW97;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=AC625_16395 {ECO:0000313|EMBL:KMY50908.1};
OS Peribacillus loiseleuriae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=1679170 {ECO:0000313|EMBL:KMY50908.1, ECO:0000313|Proteomes:UP000037146};
RN [1] {ECO:0000313|Proteomes:UP000037146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27997 {ECO:0000313|Proteomes:UP000037146};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-2015) 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 -!- 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:KMY50908.1}.
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DR EMBL; LFZW01000001; KMY50908.1; -; Genomic_DNA.
DR RefSeq; WP_049682257.1; NZ_LFZW01000001.1.
DR AlphaFoldDB; A0A0K9GW97; -.
DR STRING; 1679170.AC625_16395; -.
DR PATRIC; fig|1679170.3.peg.3727; -.
DR OrthoDB; 27330at2; -.
DR Proteomes; UP000037146; 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:UP000037146};
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..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01140"
FT TOPO_DOM 34..311
FT /note="Extracellular"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01140"
FT DOMAIN 87..229
FT /note="Cell envelope-related transcriptional attenuator"
FT /evidence="ECO:0000259|Pfam:PF03816"
SQ SEQUENCE 311 AA; 35343 MW; 87929A7D7FC1BABD CRC64;
MKRQDKTKKK KNWLKIIVIT LLIFLVAGGA YAYSIYHSLT KAVETMHTPI ENRPISDKRQ
NEIAYTNQEP FSVLLLGVDE REGDSGRSDT IIALTVNPET NSVKMLSIPR DTRTDIIGKN
KVDKINHAYA FGGVKMSMDT VENFIDIPLD YYVKINMEGF KDIVDSIGGV EVNNDLDFSS
EGDHFPIGKI KLNGAEALNF SRMRYEDPRG DFGRQYRQRE IIQGIINKGA SFATLTNYST
IFDTLSKNIE TNLTFSQMND IQKNYRAAAK NVEQIEIKST GKKIDGIYYG IVSNEEKQRI
HDELKVHLEL K
//
