TAGO_BACSU
ID TAGO_BACSU Reviewed; 358 AA.
AC O34753;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable undecaprenyl-phosphate N-acetylglucosaminyl 1-phosphate transferase;
DE EC=2.7.8.33;
DE AltName: Full=UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase;
DE AltName: Full=Undecaprenyl-Phosphate GlcNAc-1-phosphate transferase;
GN Name=tagO; Synonyms=yvhI; OrderedLocusNames=BSU35530;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=168;
RX PubMed=12101296; DOI=10.1099/00221287-148-7-2079;
RA Soldo B., Lazarevic V., Karamata D.;
RT "tagO is involved in the synthesis of all anionic cell-wall polymers in
RT Bacillus subtilis 168.";
RL Microbiology 148:2079-2087(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Catalyzes the formation of undecaprenyl-PP-N-
CC acetylglucosamine. Involved in the synthesis of anionic cell-wall
CC polymers as it mediates the initiation of the linkage unit formation
CC that appears to be common to the two types of teichoic acids attached
CC to the peptidoglycan of B.subtilis; may also be involved in teichuronic
CC acid biosynthesis (Probable). {ECO:0000305|PubMed:12101296}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-
CC D-glucosamine = N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-
CC undecaprenyl diphosphate + UMP; Xref=Rhea:RHEA:28090,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57865, ChEBI:CHEBI:60392,
CC ChEBI:CHEBI:62959; EC=2.7.8.33;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Cell wall biogenesis; poly(glucopyranosyl N-
CC acetylgalactosamine 1-phosphate) teichoic acid biosynthesis.
CC -!- PATHWAY: Cell wall biogenesis; poly(glycerol phosphate) teichoic acid
CC biosynthesis.
CC -!- INTERACTION:
CC O34753; Q01467: mreD; NbExp=3; IntAct=EBI-6401688, EBI-5246853;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. {ECO:0000305}.
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DR EMBL; AJ004803; CAA06152.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15570.1; -; Genomic_DNA.
DR PIR; B69721; B69721.
DR RefSeq; NP_391433.1; NC_000964.3.
DR RefSeq; WP_003227975.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O34753; -.
DR SMR; O34753; -.
DR IntAct; O34753; 5.
DR STRING; 224308.BSU35530; -.
DR PaxDb; O34753; -.
DR PRIDE; O34753; -.
DR EnsemblBacteria; CAB15570; CAB15570; BSU_35530.
DR GeneID; 936757; -.
DR KEGG; bsu:BSU35530; -.
DR PATRIC; fig|224308.179.peg.3844; -.
DR eggNOG; COG0472; Bacteria.
DR InParanoid; O34753; -.
DR OMA; MCLGFLP; -.
DR PhylomeDB; O34753; -.
DR BioCyc; BSUB:BSU35530-MON; -.
DR BioCyc; MetaCyc:BSU35530-MON; -.
DR BRENDA; 2.7.8.33; 658.
DR UniPathway; UPA00789; -.
DR UniPathway; UPA00827; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:InterPro.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; ISS:UniProtKB.
DR GO; GO:0036380; F:UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0044038; P:cell wall macromolecule biosynthetic process; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IBA:GO_Central.
DR GO; GO:0019350; P:teichoic acid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS.
DR PANTHER; PTHR22926; PTHR22926; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW Magnesium; Manganese; Membrane; Reference proteome;
KW Teichoic acid biosynthesis; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..358
FT /note="Probable undecaprenyl-phosphate N-acetylglucosaminyl
FT 1-phosphate transferase"
FT /id="PRO_0000108939"
FT TRANSMEM 10..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 94
FT /note="Important in orienting the substrate"
FT /evidence="ECO:0000250"
FT SITE 95
FT /note="Important in orienting the substrate; probably
FT interacts with magnesium or manganese"
FT /evidence="ECO:0000250"
FT SITE 159
FT /note="Could be required for catalysis"
FT /evidence="ECO:0000250"
FT SITE 162
FT /note="Could be required for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 358 AA; 39363 MW; A9A2941127077AAF CRC64;
MLDERMIRIV VAFIVSLLTV LIITPIVKRI AIKIGAVDQP SNRKVHDKIM PRMGGLAIFI
GVVAGVLASG IYTETRMTAI TVGAFIIIVL GILDDKYQLS AKVKFLIQLG VAIMIVSTGL
KMDFFSVPFL TERFELGWMA YPLTVLWIVG ITNAINLIDG LDGLAAGLSV IGLSTIAVMA
LSGGKVLILS LSLVVIASTL GFLFYNFHPA KIFMGDTGSL FLGYSISILS LLGLYKSVTL
FSIVIPIIIL GVPIFDTTFA IIRRILNKQP ISAPDKSHIH HRLMAFGLSH RMSVLVIYLI
GFIFSISAIV LKSATIWLSL FIIFILIIFM QIIAEVTGLV NEKFKPFTKF YKRLVKRN
