MURG_PSEAE
ID MURG_PSEAE Reviewed; 357 AA.
AC Q9HW01;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase {ECO:0000255|HAMAP-Rule:MF_00033};
DE EC=2.4.1.227 {ECO:0000255|HAMAP-Rule:MF_00033, ECO:0000305|PubMed:22973843};
DE AltName: Full=Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase {ECO:0000255|HAMAP-Rule:MF_00033};
GN Name=murG {ECO:0000255|HAMAP-Rule:MF_00033, ECO:0000303|PubMed:22973843};
GN OrderedLocusNames=PA4412;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2] {ECO:0007744|PDB:3S2U}
RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) IN COMPLEX WITH
RP UDP-N-ACETYL-ALPHA-D-GLUCOSAMINE, AND CATALYTIC ACTIVITY.
RX PubMed=22973843; DOI=10.2174/0929866511320090006;
RA Brown K., Vial S.C., Dedi N., Westcott J., Scally S., Bugg T.D.,
RA Charlton P.A., Cheetham G.M.;
RT "Crystal structure of the Pseudomonas aeruginosa MurG: UDP-GlcNAc substrate
RT complex.";
RL Protein Pept. Lett. 20:1002-1008(2013).
CC -!- FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc
CC subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid
CC intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-
CC (pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000255|HAMAP-
CC Rule:MF_00033}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-
CC muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-
CC alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-
CC undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-
CC acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-
CC D-alanyl-D-alanine + H(+) + UDP; Xref=Rhea:RHEA:31227,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:61387, ChEBI:CHEBI:61388; EC=2.4.1.227;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00033,
CC ECO:0000305|PubMed:22973843};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00033}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00033}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00033}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00033}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. MurG
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00033}.
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DR EMBL; AE004091; AAG07800.1; -; Genomic_DNA.
DR PIR; E83094; E83094.
DR RefSeq; NP_253102.1; NC_002516.2.
DR RefSeq; WP_003103107.1; NZ_QZGE01000004.1.
DR PDB; 3S2U; X-ray; 2.23 A; A=1-357.
DR PDBsum; 3S2U; -.
DR AlphaFoldDB; Q9HW01; -.
DR SMR; Q9HW01; -.
DR STRING; 287.DR97_1590; -.
DR CAZy; GT28; Glycosyltransferase Family 28.
DR PaxDb; Q9HW01; -.
DR PRIDE; Q9HW01; -.
DR DNASU; 881264; -.
DR EnsemblBacteria; AAG07800; AAG07800; PA4412.
DR GeneID; 881264; -.
DR KEGG; pae:PA4412; -.
DR PATRIC; fig|208964.12.peg.4621; -.
DR PseudoCAP; PA4412; -.
DR HOGENOM; CLU_037404_2_0_6; -.
DR InParanoid; Q9HW01; -.
DR OMA; AADMMLC; -.
DR PhylomeDB; Q9HW01; -.
DR BioCyc; PAER208964:G1FZ6-4499-MON; -.
DR BRENDA; 2.4.1.227; 5087.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0051991; F:UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol 4-beta-N-acetylglucosaminlytransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0050511; F:undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030259; P:lipid glycosylation; IEA:UniProtKB-UniRule.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR HAMAP; MF_00033; MurG; 1.
DR InterPro; IPR006009; GlcNAc_MurG.
DR InterPro; IPR007235; Glyco_trans_28_C.
DR InterPro; IPR004276; GlycoTrans_28_N.
DR Pfam; PF04101; Glyco_tran_28_C; 1.
DR Pfam; PF03033; Glyco_transf_28; 1.
DR TIGRFAMs; TIGR01133; murG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell inner membrane;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW Glycosyltransferase; Membrane; Peptidoglycan synthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..357
FT /note="UDP-N-acetylglucosamine--N-acetylmuramyl-
FT (pentapeptide) pyrophosphoryl-undecaprenol N-
FT acetylglucosamine transferase"
FT /id="PRO_0000109197"
FT BINDING 12..14
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033,
FT ECO:0000269|PubMed:22973843, ECO:0007744|PDB:3S2U"
FT BINDING 124
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033,
FT ECO:0000269|PubMed:22973843, ECO:0007744|PDB:3S2U"
FT BINDING 163
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033,
FT ECO:0000269|PubMed:22973843, ECO:0007744|PDB:3S2U"
FT BINDING 189
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033,
FT ECO:0000269|PubMed:22973843, ECO:0007744|PDB:3S2U"
FT BINDING 243
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033,
FT ECO:0000269|PubMed:22973843, ECO:0007744|PDB:3S2U"
FT BINDING 262..267
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033,
FT ECO:0000269|PubMed:22973843, ECO:0007744|PDB:3S2U"
FT BINDING 288
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033,
FT ECO:0000269|PubMed:22973843, ECO:0007744|PDB:3S2U"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:3S2U"
FT HELIX 13..28
FT /evidence="ECO:0007829|PDB:3S2U"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:3S2U"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:3S2U"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:3S2U"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3S2U"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:3S2U"
FT HELIX 74..91
FT /evidence="ECO:0007829|PDB:3S2U"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:3S2U"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3S2U"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:3S2U"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:3S2U"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:3S2U"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:3S2U"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:3S2U"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:3S2U"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:3S2U"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:3S2U"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:3S2U"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:3S2U"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:3S2U"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:3S2U"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:3S2U"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:3S2U"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:3S2U"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:3S2U"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:3S2U"
FT HELIX 262..271
FT /evidence="ECO:0007829|PDB:3S2U"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:3S2U"
FT HELIX 287..296
FT /evidence="ECO:0007829|PDB:3S2U"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:3S2U"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:3S2U"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:3S2U"
FT HELIX 311..323
FT /evidence="ECO:0007829|PDB:3S2U"
FT HELIX 326..337
FT /evidence="ECO:0007829|PDB:3S2U"
FT HELIX 343..354
FT /evidence="ECO:0007829|PDB:3S2U"
SQ SEQUENCE 357 AA; 37799 MW; 2055F342976C9387 CRC64;
MKGNVLIMAG GTGGHVFPAL ACAREFQARG YAVHWLGTPR GIENDLVPKA GLPLHLIQVS
GLRGKGLKSL VKAPLELLKS LFQALRVIRQ LRPVCVLGLG GYVTGPGGLA ARLNGVPLVI
HEQNAVAGTA NRSLAPIARR VCEAFPDTFP ASDKRLTTGN PVRGELFLDA HARAPLTGRR
VNLLVLGGSL GAEPLNKLLP EALAQVPLEI RPAIRHQAGR QHAEITAERY RTVAVEADVA
PFISDMAAAY AWADLVICRA GALTVSELTA AGLPAFLVPL PHAIDDHQTR NAEFLVRSGA
GRLLPQKSTG AAELAAQLSE VLMHPETLRS MADQARSLAK PEATRTVVDA CLEVARG
