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Database: UniProt
Entry: F0EKB7_ENTCA
LinkDB: F0EKB7_ENTCA
Original site: F0EKB7_ENTCA 
ID   F0EKB7_ENTCA            Unreviewed;       310 AA.
AC   F0EKB7;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=lytR {ECO:0000313|EMBL:EGC69575.1};
GN   Synonyms=tagU {ECO:0000256|HAMAP-Rule:MF_01140};
GN   ORFNames=HMPREF9087_1859 {ECO:0000313|EMBL:EGC69575.1};
OS   Enterococcus casseliflavus ATCC 12755.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=888066 {ECO:0000313|EMBL:EGC69575.1, ECO:0000313|Proteomes:UP000004835};
RN   [1] {ECO:0000313|EMBL:EGC69575.1, ECO:0000313|Proteomes:UP000004835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12755 {ECO:0000313|EMBL:EGC69575.1,
RC   ECO:0000313|Proteomes:UP000004835};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JAN-2011) 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:EGC69575.1}.
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DR   EMBL; AEWT01000013; EGC69575.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0EKB7; -.
DR   HOGENOM; CLU_016455_2_2_9; -.
DR   Proteomes; UP000004835; 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|HAMAP-Rule:MF_01140};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01140, ECO:0000256|SAM:Phobius};
KW   Signal-anchor {ECO:0000256|HAMAP-Rule:MF_01140};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01140};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01140, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01140,
KW   ECO:0000256|SAM:Phobius}.
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01140"
FT   TRANSMEM        7..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TOPO_DOM        28..310
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01140"
FT   DOMAIN          84..227
FT                   /note="Cell envelope-related transcriptional attenuator"
FT                   /evidence="ECO:0000259|Pfam:PF03816"
SQ   SEQUENCE   310 AA;  34738 MW;  768BB0C937D45451 CRC64;
     MSKGKKIFLI IFSIVAVLVI GMIGVAAKLY FDVSNSIQET YQSVERDRED RLRENDVDLS
     QKDSFSVLLM GIDTGDLGRV EQGRSDTMMV ATISPQDNQT TVVSIGRDSY VDIVGHGTTD
     KINHAYAFGG PAMAMNTVEK FLDIPIDHYV SINMAGLKEL VDAVGGIEVD NEITFSQDGF
     DFAIGRTSLN GEQALAYSRM RYEDPNGDYG RQERQRKIVE GIVKKVLSLD GITQYQTILN
     AVEQNMKTDM SFDDMRTLAF NYRSAFQTIK QDQLQGEGFM QDGISYQRVS DEELARVQKE
     LKAQLNLENE
//
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