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Database: UniProt
Entry: A0A1G2FMA5_9BACT
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ID   A0A1G2FMA5_9BACT        Unreviewed;       380 AA.
AC   A0A1G2FMA5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=A3E90_03520 {ECO:0000313|EMBL:OGZ38661.1};
OS   Candidatus Portnoybacteria bacterium RIFCSPHIGHO2_12_FULL_40_11.
OC   Bacteria; Candidatus Portnoybacteria.
OX   NCBI_TaxID=1801998 {ECO:0000313|EMBL:OGZ38661.1, ECO:0000313|Proteomes:UP000177247};
RN   [1] {ECO:0000313|EMBL:OGZ38661.1, ECO:0000313|Proteomes:UP000177247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:OGZ38661.1}.
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DR   EMBL; MHNC01000020; OGZ38661.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2FMA5; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000177247; 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:SF27; UDP-N-ACETYLGLUCOSAMINE--N-ACETYLMURAMYL-(PENTAPEPTIDE) PYROPHOSPHORYL-UNDECAPRENOL N-ACETYLGLUCOSAMINE TRANSFERASE; 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          3..145
FT                   /note="Glycosyltransferase family 28 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03033"
FT   DOMAIN          203..360
FT                   /note="Glycosyl transferase family 28 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04101"
FT   BINDING         10..12
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT   BINDING         168
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT   BINDING         210
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT   BINDING         310
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
SQ   SEQUENCE   380 AA;  42340 MW;  DF263AA1BDE972EE CRC64;
     MRILFTGGGS GGHLSPITAV ARQLKEIASE KNIDLRLFYL GPSDFVNEFL EKEDIKVKTI
     LAGKLRRYFS FKTILDILKI PIGLIQAILF VYAWMPDVIF SKGGYGSVPA VFAGWLFRIP
     ILIHESDAIP GLANRLGGRL VKKIALSFSS SKKYFPLEKT ALIGNPIRLD LSYKNKEEGR
     KVFEISSDKP SAFSSEKVMD KPIILIMGSS QGAEAINEMV LKTLSQLLEK YEIIHICGQK
     NYEKHKEKIG PTLPKEYHLY PFLREDQLRY GYTLADLIIS RAGASSIFEI AAAQKPSILI
     PLPTAASDHQ RENAFEYAKS GGAVILEQTN LTPHLFLTEI SRILDNQELA QKMGEGAKSF
     STPEAGQKIA EELLNLLKYC
//
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