AGGDS_STRR6
ID AGGDS_STRR6 Reviewed; 374 AA.
AC Q8DPV9; G8K019; O06452; Q7D4B3;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Alpha-galactosylglucosyldiacylglycerol synthase;
DE EC=2.4.1.-;
GN Name=cpoA; OrderedLocusNames=spr0981;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN ANTIBIOTIC RESISTANCE, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=9150233; DOI=10.1128/jb.179.10.3342-3349.1997;
RA Grebe T., Paik J., Hakenbeck R.;
RT "A novel resistance mechanism against beta-lactams in Streptococcus
RT pneumoniae involves CpoA, a putative glycosyltransferase.";
RL J. Bacteriol. 179:3342-3349(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND ACTIVITY
RP REGULATION.
RC STRAIN=CCUG 3030;
RX PubMed=12464611; DOI=10.1074/jbc.m211492200;
RA Edman M., Berg S., Storm P., Wikstrom M., Vikstrom S., Ohman A.,
RA Wieslander A.;
RT "Structural features of glycosyltransferases synthesizing major bilayer and
RT nonbilayer-prone membrane lipids in Acholeplasma laidlawii and
RT Streptococcus pneumoniae.";
RL J. Biol. Chem. 278:8420-8428(2003).
CC -!- FUNCTION: Galactosyltransferase involved in the biosynthesis of the
CC bilayer-forming membrane lipid alpha-galactosyl-glucosyldiacylglycerol
CC which is involved in maintaining constant nonbilayer/bilayer conditions
CC (curvature packing stress). Also involved in the beta-lactam
CC resistance. Catalyzes the transfer of a galactosyl residue from UDP-Gal
CC to alpha-glucosyl-DAG (1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-
CC glycerol) acceptor to form the corresponding galactosyl-glycosyl-DAG
CC product (3-O-alpha-(D-galactopyranosyl-alpha-(1->2)-D-glucopyranosyl)-
CC 1,2-diacyl-sn-glycerol). It can only use UDP-Gal as sugar donor and
CC alpha-glucosyl-DAG is the preferred sugar acceptor.
CC {ECO:0000269|PubMed:12464611, ECO:0000269|PubMed:9150233}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol + UDP-
CC alpha-D-galactose = a 1,2-diacyl-3-O-[alpha-D-galactopyranosyl-
CC (1->2)-alpha-D-glucopyranosyl]-sn-glycerol + H(+) + UDP;
CC Xref=Rhea:RHEA:52696, ChEBI:CHEBI:15378, ChEBI:CHEBI:17670,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:136769;
CC Evidence={ECO:0000269|PubMed:12464611};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by the negatively charged lipid
CC phosphatidylglycerol (PG). {ECO:0000269|PubMed:12464611}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9150233}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR EMBL; Y11463; CAA72249.1; -; Genomic_DNA.
DR EMBL; AE007317; AAK99785.1; -; Genomic_DNA.
DR PIR; E97994; E97994.
DR RefSeq; NP_358575.1; NC_003098.1.
DR RefSeq; WP_010976517.1; NC_003098.1.
DR AlphaFoldDB; Q8DPV9; -.
DR SMR; Q8DPV9; -.
DR STRING; 171101.spr0981; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR EnsemblBacteria; AAK99785; AAK99785; spr0981.
DR GeneID; 60232782; -.
DR KEGG; spr:spr0981; -.
DR PATRIC; fig|171101.6.peg.1067; -.
DR eggNOG; COG0438; Bacteria.
DR HOGENOM; CLU_055069_1_0_9; -.
DR OMA; GQVQERK; -.
DR BioCyc; MetaCyc:MON-20029; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016758; F:hexosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046467; P:membrane lipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Carbohydrate metabolism; Cell membrane;
KW Glycerol metabolism; Glycosyltransferase; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Membrane; Reference proteome; Transferase.
FT CHAIN 1..374
FT /note="Alpha-galactosylglucosyldiacylglycerol synthase"
FT /id="PRO_0000425271"
FT CONFLICT 246
FT /note="T -> K (in Ref. 1; CAA72249)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 43093 MW; 03D9D0642D1470B2 CRC64;
MRKFPLFSSS LSFLLLILFK ENDIIVVMEK KKLRINMLSS SEKVAGQGVS GAYRELVRLL
HRAAKDQLIV TENLPIEADV THFHTIDFPY YLSTFQKKRS GRKIGYVHFL PATLEGSLKI
PFFLKGIVKR YVFSFYNRME HLVVVNPMFI EDLVAAGIPR EKVTYIPNFV NKEKWHPLPQ
EEVVRLRTDL GLSDNQFIVV GAGQVQKRKG IDDFIRLAEE LPQITFIWAG GFSFGGMTDG
YEHYKTIMEN PPKNLIFPGI VSPERMRELY ALADLFLLPS YNELFPMTIL EAASCEAPIM
LRDLDLYKVI LEGNYRATAG REEMKEAILE YQANPAVLKD LKEKAKNISR EYSEEHLLQI
WLDFYEKQAA LGRK
