ID A0A291R0Z1_9BACT Unreviewed; 406 AA.
AC A0A291R0Z1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=4,4'-diaponeurosporenoate glycosyltransferase {ECO:0000256|ARBA:ARBA00040345};
GN ORFNames=COR50_10730 {ECO:0000313|EMBL:ATL49821.1};
OS Chitinophaga caeni.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=2029983 {ECO:0000313|EMBL:ATL49821.1, ECO:0000313|Proteomes:UP000220133};
RN [1] {ECO:0000313|EMBL:ATL49821.1, ECO:0000313|Proteomes:UP000220133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 {ECO:0000313|EMBL:ATL49821.1,
RC ECO:0000313|Proteomes:UP000220133};
RA Jin D., Kong X., Deng Y., Bai Z.;
RT "Paenichitinophaga pekingensis gen. nov., sp. nov., isolated from activated
RT sludge.";
RL Submitted (OCT-2017) 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 -!- PATHWAY: Carotenoid biosynthesis; staphyloxanthin biosynthesis;
CC staphyloxanthin from farnesyl diphosphate: step 4/5.
CC {ECO:0000256|ARBA:ARBA00037904}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. CrtQ
CC subfamily. {ECO:0000256|ARBA:ARBA00038120}.
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DR EMBL; CP023777; ATL49821.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291R0Z1; -.
DR KEGG; cbae:COR50_10730; -.
DR OrthoDB; 9810303at2; -.
DR Proteomes; UP000220133; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd04179; DPM_DPG-synthase_like; 1.
DR InterPro; IPR018639; DUF2062.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10859:SF91; DOLICHYL-PHOSPHATE BETA-GLUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR10859; GLYCOSYL TRANSFERASE; 1.
DR Pfam; PF09835; DUF2062; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000220133};
KW Transferase {ECO:0000313|EMBL:ATL49821.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 224..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..132
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT DOMAIN 262..393
FT /note="DUF2062"
FT /evidence="ECO:0000259|Pfam:PF09835"
SQ SEQUENCE 406 AA; 46082 MW; 0865E4CE3A453586 CRC64;
MQTFETYHPK FTALKTCVLI PTYNNAGTLA QVVEDVLCYT QHVIVVNDGA TDETATILTA
FPQVKVISYQ PNKGKGWALR TGFKAAVELG YDYAITIDAD GQHFASDLPI MLQQVEEQPG
TLVIGARNLQ EENMPGKNTF ANKFSNFWFY VETGKKAADT QSGYRLYPLY RMKKIGFWCR
KYEFEVEVLV RSSWRGIPIA WVPVKVYYPP AEERVSHFRP FRDFSRISVL NTVLVTIAFL
YIKPRDFFRY IAKAENRKAL FREHLWNSNE SNSKKALAIG LGIFMGIVPI WGFQMMAAFA
LATLFKLNKA LVILAANISI PPMVPLIIYG SFLAGKIWVK EDLTGQVFSR SFSWEAVKQG
GLQYISGAFT LAFIAGILAW LITYLLLVMV RRKPTTHRHF QNGSSR
//