ID A0A0Q7NIX7_9NOCA Unreviewed; 425 AA.
AC A0A0Q7NIX7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=4,4'-diaponeurosporenoate glycosyltransferase {ECO:0000256|ARBA:ARBA00040345};
DE EC=2.4.1.117 {ECO:0000256|ARBA:ARBA00012583};
GN ORFNames=ASD42_13665 {ECO:0000313|EMBL:KQY39285.1};
OS Nocardia sp. Root136.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1736458 {ECO:0000313|EMBL:KQY39285.1, ECO:0000313|Proteomes:UP000051507};
RN [1] {ECO:0000313|Proteomes:UP000051507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root136 {ECO:0000313|Proteomes:UP000051507};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY39285.1, ECO:0000313|Proteomes:UP000051507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root136 {ECO:0000313|EMBL:KQY39285.1,
RC ECO:0000313|Proteomes:UP000051507};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the glycosylation of 4,4'-diaponeurosporenoate,
CC i.e. the esterification of glucose at the C1'' position with the
CC carboxyl group of 4,4'-diaponeurosporenic acid, to form glycosyl-4,4'-
CC diaponeurosporenoate. This is a step in the biosynthesis of
CC staphyloxanthin, an orange pigment present in most staphylococci
CC strains. {ECO:0000256|ARBA:ARBA00037281}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl phosphate + UDP-alpha-D-glucose = a dolichyl beta-
CC D-glucosyl phosphate + UDP; Xref=Rhea:RHEA:15401, Rhea:RHEA-
CC COMP:9517, Rhea:RHEA-COMP:9528, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.117;
CC Evidence={ECO:0000256|ARBA:ARBA00034053};
CC -!- PATHWAY: Carotenoid biosynthesis; staphyloxanthin biosynthesis;
CC staphyloxanthin from farnesyl diphosphate: step 4/5.
CC {ECO:0000256|ARBA:ARBA00037904}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004648}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. CrtQ
CC subfamily. {ECO:0000256|ARBA:ARBA00038120}.
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:KQY39285.1}.
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DR EMBL; LMFE01000001; KQY39285.1; -; Genomic_DNA.
DR RefSeq; WP_056814924.1; NZ_LMFE01000001.1.
DR AlphaFoldDB; A0A0Q7NIX7; -.
DR STRING; 1736458.ASD42_13665; -.
DR Proteomes; UP000051507; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
DR CDD; cd04188; DPG_synthase; 1.
DR InterPro; IPR035518; DPG_synthase.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR007267; GtrA_DPMS_TM.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10859:SF91; DOLICHYL-PHOSPHATE BETA-GLUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR10859; GLYCOSYL TRANSFERASE; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF04138; GtrA; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 279..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..187
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT DOMAIN 281..397
FT /note="GtrA/DPMS transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04138"
SQ SEQUENCE 425 AA; 45686 MW; 68119EFF127DA30C CRC64;
MTQTEAEQKA MQSSRAPVLD VVIPVYNEEV DLGLCVRRLH SYLRAGFPFT ARITIADNAS
TDATLAVAEL LAAELDGVQV LHLDAKGRGR ALRTAWEGSD AAVVAYMDVD LSTDLNALLP
LIAPLVSGHS DLAIGTRLDS SSRVVRGPKR EIISRCYNLL LKTTLRAGFS DAQCGFKAVR
TEVARELLPL VRDGEWFFDT ELLVLAERAG LRIHEVPVDW IDDPDSRVDI IDTARKDLRG
IWRLTRALTT GALPVDELRA AVGREPLVAG VPLGMVGQLV RFAIVGVTST LAYIALYLLL
QPLVGSQGAN LVSLLITAVG NTAANRAFTF GVRGRGNAVS HQFQGLAIFA FGLAITSGSL
FALHRWAPDA PVAVELTVLI TANLVATLAR FVGLRWVFRH AGVGDATVTP VVGSAERMSA
LGVRR
//