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Database: UniProt
Entry: N9FQT6_9GAMM
LinkDB: N9FQT6_9GAMM
Original site: N9FQT6_9GAMM 
ID   N9FQT6_9GAMM            Unreviewed;       352 AA.
AC   N9FQT6;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase {ECO:0000256|HAMAP-Rule:MF_00033};
DE            EC=2.4.1.227 {ECO:0000256|HAMAP-Rule:MF_00033};
DE   AltName: Full=Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase {ECO:0000256|HAMAP-Rule:MF_00033};
GN   Name=murG {ECO:0000256|HAMAP-Rule:MF_00033};
GN   ORFNames=F933_01652 {ECO:0000313|EMBL:ENW07184.1};
OS   Acinetobacter beijerinckii CIP 110307.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1217648 {ECO:0000313|EMBL:ENW07184.1, ECO:0000313|Proteomes:UP000017670};
RN   [1] {ECO:0000313|EMBL:ENW07184.1, ECO:0000313|Proteomes:UP000017670}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 110307 {ECO:0000313|EMBL:ENW07184.1,
RC   ECO:0000313|Proteomes:UP000017670};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter beijerinckii CIP 110307.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00033};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00033}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00033};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00033};
CC       Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00033}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. MurG
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00033}.
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:ENW07184.1}.
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DR   EMBL; APQL01000005; ENW07184.1; -; Genomic_DNA.
DR   AlphaFoldDB; N9FQT6; -.
DR   STRING; 262668.GCA_000931715_01980; -.
DR   PATRIC; fig|1217648.3.peg.1620; -.
DR   eggNOG; COG0707; Bacteria.
DR   HOGENOM; CLU_037404_2_0_6; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000017670; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
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   CDD; cd03785; GT28_MurG; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
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   NCBIfam; TIGR01133; murG; 1.
DR   PANTHER; PTHR21015:SF22; GLYCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR21015; UDP-N-ACETYLGLUCOSAMINE--N-ACETYLMURAMYL-(PENTAPEPTIDE) PYROPHOSPHORYL-UNDECAPRENOL N-ACETYLGLUCOSAMINE TRANSFERASE 1; 1.
DR   Pfam; PF04101; Glyco_tran_28_C; 1.
DR   Pfam; PF03033; Glyco_transf_28; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00033};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00033};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00033};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00033};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00033};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00033};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00033};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00033};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00033}.
FT   DOMAIN          1..136
FT                   /note="Glycosyltransferase family 28 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03033"
FT   DOMAIN          182..343
FT                   /note="Glycosyl transferase family 28 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04101"
FT   BINDING         6..8
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT   BINDING         118
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT   BINDING         157
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT   BINDING         188
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT   BINDING         242
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT   BINDING         261..266
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT   BINDING         287
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
SQ   SEQUENCE   352 AA;  37898 MW;  E28414E9DF0F32A8 CRC64;
     MMAAGTGGHV FPALAVAKQL QQEGCQVSWL ATPTGMENRL LKDQNIPIYQ IDIQGVRGNG
     LLRKLSAPFK ILKATLSAMR YMKQLNIDAV AGFGGYVAGP GGLAARLLGI PVLIHEQNAI
     AGFTNTQLSR IAKTVCQAFP NTFPTSDKVV TTGNPVRAEI TAILNPSWRY QTREQEQLPI
     NILIVGGSLG AQALNERLPE ALKKVNIPLN VFHQCGQNQQ DATRVRYQGA SQSLNIQVEP
     FIHDMAKAYS EADLIICRAG ALTVTEVATA GLAAVFVPLP IAVDDHQTAN AKFLANVGAA
     KICQQADMTP AVLDELLATL LNRQLLSEMA IKARQQAQPN ATQHVVDLIK KL
//
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