(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BI67_GEOS0

ID   A0A0F6BI67_GEOS0        Unreviewed;       235 AA.
AC   A0A0F6BI67;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 21.
DE   RecName: Full=N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase {ECO:0000256|HAMAP-Rule:MF_02070};
DE            EC=2.4.1.187 {ECO:0000256|HAMAP-Rule:MF_02070};
DE   AltName: Full=N-acetylmannosaminyltransferase {ECO:0000256|HAMAP-Rule:MF_02070};
DE   AltName: Full=UDP-N-acetylmannosamine transferase {ECO:0000256|HAMAP-Rule:MF_02070};
DE   AltName: Full=UDP-N-acetylmannosamine:N-acetylglucosaminyl pyrophosphorylundecaprenol N-acetylmannosaminyltransferase {ECO:0000256|HAMAP-Rule:MF_02070};
GN   OrderedLocusNames=GY4MC1_0270 {ECO:0000313|EMBL:ADP73118.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73118.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73118.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73118.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of GlcNAc-PP-undecaprenol into
CC       ManNAc-GlcNAc-PP-undecaprenol, the first committed lipid
CC       intermediate in the de novo synthesis of teichoic acid.
CC       {ECO:0000256|HAMAP-Rule:MF_02070}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-alpha-D-glucosaminyl-1-diphospho-di-trans,octa-
CC         cis-undecaprenol + UDP-N-acetyl-alpha-D-mannosamine = H(+) + N-
CC         acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl
CC         di-trans,octa-cis-undecaprenyl diphosphate + UDP;
CC         Xref=Rhea:RHEA:16053, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:62959, ChEBI:CHEBI:68623, ChEBI:CHEBI:132210;
CC         EC=2.4.1.187; Evidence={ECO:0000256|HAMAP-Rule:MF_02070};
CC   -!- PATHWAY: Cell wall biogenesis; teichoic acid biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02070}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 26 family.
CC       TagA/TarA subfamily. {ECO:0000256|HAMAP-Rule:MF_02070}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002293; ADP73118.1; -; Genomic_DNA.
DR   RefSeq; WP_003247821.1; NC_014650.1.
DR   EnsemblBacteria; ADP73118; ADP73118; GY4MC1_0270.
DR   GeneID; 29237083; -.
DR   KEGG; gmc:GY4MC1_0270; -.
DR   KO; K05946; -.
DR   OMA; PWRWRRM; -.
DR   OrthoDB; 1759731at2; -.
DR   BioCyc; GSP581103:G1GOQ-313-MONOMER; -.
DR   UniPathway; UPA00632; -.
DR   Proteomes; UP000002034; Chromosome.
DR   GO; GO:0047244; F:N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0019350; P:teichoic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06533; Glyco_transf_WecG_TagA; 1.
DR   HAMAP; MF_02070; TagA_TarA; 1.
DR   InterPro; IPR034714; TagA_TarA.
DR   InterPro; IPR004629; WecB_TagA_CpsF.
DR   PANTHER; PTHR34136; PTHR34136; 1.
DR   Pfam; PF03808; Glyco_tran_WecB; 1.
DR   TIGRFAMs; TIGR00696; wecG_tagA_cpsF; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BI67.
DR   SWISS-2DPAGE; A0A0F6BI67.
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02070};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_02070,
KW   ECO:0000256|SAAS:SAAS00768725, ECO:0000313|EMBL:ADP73118.1};
KW   Teichoic acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02070};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02070,
KW   ECO:0000256|SAAS:SAAS00768714, ECO:0000313|EMBL:ADP73118.1}.
SQ   SEQUENCE   235 AA;  26755 MW;  B257D4770D347FAE CRC64;
     MKETFLGVDV CTYTYEQLVA KLMEDIDNNR KSFIVAINPE KIMKAQQDDR LRELLNQATY
     PIPDGIGVVL ASILKRGRIR SRVTGIDMML RLCQEAAARG KKIFLYGAKP GVADEAKRRL
     EKMFPGIQIV GTMHGYEKDE QVIKEAINQS GADILFVALG SPAQEYWIAN HMHSLSPKVY
     QGVGGSFDVI SGRIKRAPLL VQKLGLEWLY RLLKEPWRWK RQLALPKFLI KVIRE
//

If you have problems or comments...

PBIL Back to PBIL home page