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Database: UniProt
Entry: A0A021WXC7_9RHIZ
LinkDB: A0A021WXC7_9RHIZ
Original site: A0A021WXC7_9RHIZ 
ID   A0A021WXC7_9RHIZ        Unreviewed;       378 AA.
AC   A0A021WXC7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   11-DEC-2019, entry version 42.
DE   RecName: Full=UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase {ECO:0000256|HAMAP-Rule:MF_00033, ECO:0000256|SAAS:SAAS00082867};
DE            EC=2.4.1.227 {ECO:0000256|HAMAP-Rule:MF_00033, ECO:0000256|SAAS:SAAS00082938};
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   ECO:0000313|EMBL:EYR77748.1};
GN   ORFNames=SHLA_21c000480 {ECO:0000313|EMBL:EYR77748.1};
OS   Shinella sp. DD12.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Rhizobiaceae;
OC   Shinella; unclassified Shinella.
OX   NCBI_TaxID=1410620 {ECO:0000313|EMBL:EYR77748.1, ECO:0000313|Proteomes:UP000017832};
RN   [1] {ECO:0000313|EMBL:EYR77748.1, ECO:0000313|Proteomes:UP000017832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD12 {ECO:0000313|EMBL:EYR77748.1,
RC   ECO:0000313|Proteomes:UP000017832};
RA   Poehlein A., Freese H., Daniel R., Simeonova D.D.;
RT   "Draft Genome Sequence of Shinella sp. DD12.";
RL   Submitted (JAN-2014) 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, ECO:0000256|SAAS:SAAS00082940}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-
CC         trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-glucosamine =
CC         beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
CC         diphospho-di-trans,octa-cis-undecaprenol + H(+) + UDP;
CC         Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033;
CC         EC=2.4.1.227; Evidence={ECO:0000256|HAMAP-Rule:MF_00033,
CC         ECO:0000256|SAAS:SAAS01209325};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00033, ECO:0000256|SAAS:SAAS00082937}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00033};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00033}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. MurG
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00033,
CC       ECO:0000256|SAAS:SAAS00569248}.
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:EYR77748.1}.
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DR   EMBL; AYLZ02000218; EYR77748.1; -; Genomic_DNA.
DR   RefSeq; WP_023516472.1; NZ_AYLZ02000218.1.
DR   STRING; 1410620.SHLA_21c000480; -.
DR   EnsemblBacteria; EYR77748; EYR77748; SHLA_21c000480.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000017832; 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   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   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00033,
KW   ECO:0000256|SAAS:SAAS00458215};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00033,
KW   ECO:0000256|SAAS:SAAS00458169};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00033,
KW   ECO:0000256|SAAS:SAAS00082922};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00033,
KW   ECO:0000256|SAAS:SAAS00458137};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00033,
KW   ECO:0000256|SAAS:SAAS00458192};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00033,
KW   ECO:0000256|SAAS:SAAS00458141, ECO:0000313|EMBL:EYR77748.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00033, ECO:0000256|SAAS:SAAS00458209};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00033,
KW   ECO:0000256|SAAS:SAAS00458156};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00033,
KW   ECO:0000256|SAAS:SAAS00458181, ECO:0000313|EMBL:EYR77748.1}.
FT   DOMAIN          6..142
FT                   /note="Glyco_transf_28"
FT                   /evidence="ECO:0000259|Pfam:PF03033"
FT   DOMAIN          186..350
FT                   /note="Glyco_tran_28_C"
FT                   /evidence="ECO:0000259|Pfam:PF04101"
SQ   SEQUENCE   378 AA;  39564 MW;  121572B0E369B453 CRC64;
     MNKGIVLLAA GGTGGHLFPA EALAHELKAG GWSVHLVTDS RAERFAGKFP ADEIHVVPSA
     TIGSKNPVSV VKSLFTLWRG IRVARKLMAR LKPKVVVGFG GYPTVPPLIA ATGMGIPSMI
     HEQNAVMGRA NKALANRVKA IAGGFLPETD GLYAAKTVTT GNPVRPAVLE AATIPYQAST
     DGEFRLVVFG GSQGAQFFSK AIPSAIAALE PADRMRLRIT QQARPEDRDE VVRTYGELGI
     PADVSPFFTD MAARIGNAHL VISRSGASTV SEVSVIGRPA ILVPYPYALD HDQAANAAAL
     AAGGGAKVIV QGELSTERLA SIVSKAMHDP ARMTEMAANA RKAGKPDAAR LLALMVEAIA
     GGKPIAQFKG AQFKGERP
//
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