RNTF_MYCTA
ID RNTF_MYCTA Reviewed; 449 AA.
AC A5U6X0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=PGL/p-HBAD biosynthesis rhamnosyltransferase;
DE EC=2.4.1.-;
GN OrderedLocusNames=MRA_2989;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
CC -!- FUNCTION: Catalyzes the transfer of the first rhamnosyl residue on p-
CC hydroxybenzoic acid or phenolphthiocerol derivatives to form, after O-
CC methylation at position 2 of the sugar unit, mono-O-methyl-glycosyl-p-
CC hydroxybenzoic acid derivative (p-HBAD I) and 2-O-methyl-rhamnosyl-
CC phenolphthiocerol dimycocerosate (also called mycoside B) during p-
CC hydroxybenzoic acid derivatives (p-HBAD) and glycosylated
CC phenolphthiocerol dimycocerosates (PGL) biosynthesis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000305}.
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DR EMBL; CP000611; ABQ74770.1; -; Genomic_DNA.
DR RefSeq; WP_003414922.1; NZ_CP016972.1.
DR AlphaFoldDB; A5U6X0; -.
DR SMR; A5U6X0; -.
DR STRING; 419947.MRA_2989; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR EnsemblBacteria; ABQ74770; ABQ74770; MRA_2989.
DR KEGG; mra:MRA_2989; -.
DR eggNOG; COG1819; Bacteria.
DR HOGENOM; CLU_692271_0_0_11; -.
DR OMA; WNIEECV; -.
DR OrthoDB; 1485440at2; -.
DR Proteomes; UP000001988; Chromosome.
DR GO; GO:0016758; F:hexosyltransferase activity; IEA:UniProt.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR Pfam; PF00201; UDPGT; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..449
FT /note="PGL/p-HBAD biosynthesis rhamnosyltransferase"
FT /id="PRO_0000313793"
SQ SEQUENCE 449 AA; 49433 MW; 205FDB0855C0A109 CRC64;
MRVSCVYATA SRWGGPPVAS EVRGDAAIST TPDAAPGLAA RRRRILFVAE AVTLAHVVRP
FALAQSLDPS RYEVHFACDP RYNQLLGPLP FRHHAIHTIP SERFFGNLTQ GRFYAMRTLR
KYVEADLRVL DEIAPDLVVG DLRISLSVSA RLAGIPYIAI ANAYWSPYAQ RRFPLPDVIW
TRLFGVRLVK LLYRLERPLL FALQCMPLNW VRRRHGLSSL GWNLCRIFTD GDHTLYADVP
ELMPTYDLPA NHEYLGPVLW SPAGKPPTWW DSLPTDRPIV YATLGTSGGR NLLQLVLNAL
AELPVTVIAA TAGRSDLKTV PANAFVADYL PGEAAAARSA VVVCNGGSLT TQQALVAGVP
VIGVAGNLDQ HLNMEAVERA GAGVLLRTER LKSQRVAGAV MQVISRSEYR QAAARLADAF
GRDRVGFPQH VENALRLMPE NRPRTWLAS