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Database: UniProt
Entry: U2B4N4_9CLOT
LinkDB: U2B4N4_9CLOT
Original site: U2B4N4_9CLOT 
ID   U2B4N4_9CLOT            Unreviewed;       363 AA.
AC   U2B4N4;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   26-FEB-2020, entry version 36.
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   ORFNames=HMPREF1548_00077 {ECO:0000313|EMBL:ERI73129.1};
OS   Clostridium sp. KLE 1755.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1226325 {ECO:0000313|EMBL:ERI73129.1, ECO:0000313|Proteomes:UP000016509};
RN   [1] {ECO:0000313|EMBL:ERI73129.1, ECO:0000313|Proteomes:UP000016509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLE 1755 {ECO:0000313|EMBL:ERI73129.1,
RC   ECO:0000313|Proteomes:UP000016509};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (JUN-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, 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:ERI73129.1}.
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DR   EMBL; AWST01000002; ERI73129.1; -; Genomic_DNA.
DR   RefSeq; WP_021635569.1; NZ_KE992684.1.
DR   STRING; 1226325.HMPREF1548_00077; -.
DR   EnsemblBacteria; ERI73129; ERI73129; HMPREF1548_00077.
DR   PATRIC; fig|1226325.3.peg.75; -.
DR   HOGENOM; CLU_037404_0_0_9; -.
DR   OrthoDB; 1165736at2; -.
DR   BioCyc; GCF_000466465-HMP:HMPREF1548_RS08515-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000016509; 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:ERI73129.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000016509};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00033,
KW   ECO:0000256|SAAS:SAAS00458181, ECO:0000313|EMBL:ERI73129.1}.
FT   DOMAIN          5..141
FT                   /note="Glyco_transf_28"
FT                   /evidence="ECO:0000259|Pfam:PF03033"
FT   DOMAIN          188..344
FT                   /note="Glyco_tran_28_C"
FT                   /evidence="ECO:0000259|Pfam:PF04101"
SQ   SEQUENCE   363 AA;  39871 MW;  352C8D0913C42699 CRC64;
     MSKKIVLTGG GTAGHITPNI ALLPRLSQLG YEISYIGSYN GMEKKLIEDY DIPYYGISTG
     KFRRYFDLKN FTDPFRVIKG YGEARKYLKE IRPDIVFSKG GFVSVPVVRA ASSLKIPCVI
     HESDMTPGLA NKLCIPVATK VCCNFPETLH NLPTEKAVLT GSPIRDELSK GNKLAALELC
     HFTANKPVLM VIGGSLGAAS INQAVREALP KLLNDFQIVH ICGHEKIDNL LLNQSGYAQF
     EYLKAELKDV FAMADVVVSR AGANAICELL ALKKPNLLIP LSAGSSRGDQ ILNARSFETQ
     GYSMVIDEDY LSPDLLVEKV QELYFNRQTY INAMGKSQQM NATKTITELL DGIVEENKAG
     KGK
//
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