ID W2EE25_9BACL Unreviewed; 366 AA.
AC W2EE25;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Putative undecaprenyl-phosphate N-acetylglucosaminyl 1-phosphate transferase TagO {ECO:0000313|EMBL:ETK29191.1};
GN Name=tagO1 {ECO:0000313|EMBL:ETK29191.1};
GN ORFNames=ERIC1_1c26960 {ECO:0000313|EMBL:ETK29191.1};
OS Paenibacillus larvae subsp. larvae DSM 25719.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=697286 {ECO:0000313|EMBL:ETK29191.1, ECO:0000313|Proteomes:UP000018834};
RN [1] {ECO:0000313|EMBL:ETK29191.1, ECO:0000313|Proteomes:UP000018834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25719 {ECO:0000313|EMBL:ETK29191.1,
RC ECO:0000313|Proteomes:UP000018834};
RX PubMed=24599066;
RA Djukic M., Brzuszkiewicz E., Funfhaus A., Voss J., Gollnow K., Poppinga L.,
RA Liesegang H., Garcia-Gonzalez E., Genersch E., Daniel R.;
RT "How to Kill the Honey Bee Larva: Genomic Potential and Virulence
RT Mechanisms of Paenibacillus larvae.";
RL PLoS ONE 9:E90914-E90914(2014).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR600715-1};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:ETK29191.1}.
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DR EMBL; ADFW01000001; ETK29191.1; -; Genomic_DNA.
DR RefSeq; WP_023484008.1; NZ_ADFW01000001.1.
DR AlphaFoldDB; W2EE25; -.
DR PATRIC; fig|697286.3.peg.2897; -.
DR OrthoDB; 9783652at2; -.
DR Proteomes; UP000018834; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR CDD; cd06853; GT_WecA_like; 1.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS.
DR PANTHER; PTHR22926; PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE; 1.
DR PANTHER; PTHR22926:SF3; UNDECAPRENYL-PHOSPHATE ALPHA-N-ACETYLGLUCOSAMINYL 1-PHOSPHATE TRANSFERASE; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
DR PROSITE; PS01348; MRAY_2; 1.
PE 4: Predicted;
KW Magnesium {ECO:0000256|PIRSR:PIRSR600715-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR600715-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ETK29191.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 49..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 366 AA; 39398 MW; F154665EE82067BE CRC64;
MYAFNVIGFI VACLFALLLT PLVKKFAFWV GAVDAPNHRK VHTRIMPRLG GLAIFIAFVG
AYCVISPVIG AFHTEATIPM LLGGFVIVLT GALDDRFELS PKMKLLGQLI AAIMVVVSGL
QIDVVKIPFT GSEWVIPNVI SIPLTIIWII GVSNAINLID GLDGLSAGVS GIATATMMVL
AIMMPEPTVV LFSVILLGSI VGFLFYNFHP AKIFMGDSGA LFLGYALATL SIMGFKQAAV
LSLLTPILIL GVPLSDTFFA IVRRYVNKKP ISVADKNHLH HCLLQLGFSH RTTVLIIYGI
ALFFGGCAIL FNQVGQWWAV AGVVVLSVIL IVGAEAIGII SKSRKPVLGL LQKMRMKDSL
NSRLPK
//
