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Database: UniProt
Entry: A0A0V8J529_9BACI
LinkDB: A0A0V8J529_9BACI
Original site: A0A0V8J529_9BACI 
ID   A0A0V8J529_9BACI        Unreviewed;       312 AA.
AC   A0A0V8J529;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=AS030_17175 {ECO:0000313|EMBL:KSU82011.1};
OS   Fictibacillus enclensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX   NCBI_TaxID=1017270 {ECO:0000313|EMBL:KSU82011.1, ECO:0000313|Proteomes:UP000054099};
RN   [1] {ECO:0000313|EMBL:KSU82011.1, ECO:0000313|Proteomes:UP000054099}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIO-1003 {ECO:0000313|EMBL:KSU82011.1,
RC   ECO:0000313|Proteomes:UP000054099};
RX   PubMed=24343101; DOI=10.1007/s10482-013-0097-9;
RA   Dastager S.G., Mawlankar R., Srinivasan K., Tang S.K., Lee J.C.,
RA   Ramana V.V., Shouche Y.S.;
RT   "Fictibacillus enclensis sp. nov., isolated from marine sediment.";
RL   Antonie Van Leeuwenhoek 105:461-469(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:KSU82011.1}.
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DR   EMBL; LNQN01000005; KSU82011.1; -; Genomic_DNA.
DR   RefSeq; WP_061973877.1; NZ_KQ758619.1.
DR   AlphaFoldDB; A0A0V8J529; -.
DR   OrthoDB; 27330at2; -.
DR   Proteomes; UP000054099; 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:UP000054099};
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..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01140"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TOPO_DOM        35..312
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   312 AA;  34609 MW;  8624A57280CB4102 CRC64;
     MDSRSAKRKK KRSGLKIALI VIGVIVLIAA GGIYYVYGSV KSTANKMHEG SEWNGSDKRK
     GALTPDKGDP LSILILGVDE RQGDRGRSDT LILVTVNPKT NKMVMTSIPR DTRTEIVGKG
     KEDKINHAYA FGGEKMAIKT VENFLDVPVD YYVKVNMESF QGLVDALGGV TVDNERLAFK
     YDGYNFPKGE LKLSGKEALA YTRMRKEDPQ GDFGRNARQR QVISAIINEG AQVSSVTKMG
     DILDVIGSNV KTNLTFDEMK DIQSKYKGAR NNVDNVEIKG NGQMINGIYY LIVPDEERTR
     IQTMLKEQLE IS
//
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