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Database: UniProt
Entry: A0A059KNI7_9BURK
LinkDB: A0A059KNI7_9BURK
Original site: A0A059KNI7_9BURK 
ID   A0A059KNI7_9BURK        Unreviewed;       469 AA.
AC   A0A059KNI7;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase {ECO:0000313|EMBL:KDB52945.1};
GN   ORFNames=X805_14640 {ECO:0000313|EMBL:KDB52945.1};
OS   Sphaerotilus natans subsp. natans DSM 6575.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Sphaerotilus.
OX   NCBI_TaxID=1286631 {ECO:0000313|EMBL:KDB52945.1, ECO:0000313|Proteomes:UP000026714};
RN   [1] {ECO:0000313|EMBL:KDB52945.1, ECO:0000313|Proteomes:UP000026714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6575 {ECO:0000313|EMBL:KDB52945.1,
RC   ECO:0000313|Proteomes:UP000026714};
RX   PubMed=24965827; DOI=10.1111/1574-6941.12372;
RA   Park S., Kim D.H., Lee J.H., Hur H.G.;
RT   "Sphaerotilus natans encrusted with nanoball-shaped Fe(III) oxide minerals
RT   formed by nitrate-reducing mixotrophic Fe(II) oxidation.";
RL   FEMS Microbiol. Ecol. 90:68-77(2014).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the bacterial sugar transferase family.
CC       {ECO:0000256|ARBA:ARBA00006464}.
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:KDB52945.1}.
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DR   EMBL; AZRA01000035; KDB52945.1; -; Genomic_DNA.
DR   RefSeq; WP_076458426.1; NZ_AZRA01000035.1.
DR   AlphaFoldDB; A0A059KNI7; -.
DR   STRING; 34103.SAMN05421778_1016; -.
DR   PATRIC; fig|1286631.3.peg.1447; -.
DR   eggNOG; COG1086; Bacteria.
DR   eggNOG; COG2148; Bacteria.
DR   Proteomes; UP000026714; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR003362; Bact_transf.
DR   InterPro; IPR017475; EPS_sugar_tfrase.
DR   InterPro; IPR017464; Sugar_tfrase_EpsB_2.
DR   NCBIfam; TIGR03025; EPS_sugtrans; 1.
DR   NCBIfam; TIGR03013; EpsB_2; 1.
DR   PANTHER; PTHR30576; COLANIC BIOSYNTHESIS UDP-GLUCOSE LIPID CARRIER TRANSFERASE; 1.
DR   PANTHER; PTHR30576:SF0; UNDECAPRENYL-PHOSPHATE N-ACETYLGALACTOSAMINYL 1-PHOSPHATE TRANSFERASE-RELATED; 1.
DR   Pfam; PF02397; Bac_transf; 1.
DR   Pfam; PF13727; CoA_binding_3; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KDB52945.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        48..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        85..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        282..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          280..463
FT                   /note="Bacterial sugar transferase"
FT                   /evidence="ECO:0000259|Pfam:PF02397"
SQ   SEQUENCE   469 AA;  52257 MW;  F2309EDCD510D003 CRC64;
     MFRVFQHRSS GTHFVELFAD GLLCFIAALL SAATLASPLP GVSPLTQIIT PTILLVAFSF
     ALVMALLYSF VGLYRHRNLG LVPMVVRIGF AFLLGGYITY LTLKYISYDG YAGSLVGYSL
     VYLLVGLMLY RGVAWVVRQA VGTRRVLIVG TGPDARQVCT DLRAGGQWAG YDVVGFYPTT
     EQTDRAALRG AAHVFDARQK LVDLVREHRI NEIIVAVREQ RGGGVPMNDL LECRIGGVPI
     MDLAYFYERT KAEVPVDSLK ASWLVYGDGF VQGHARELTK RLFDIVSSSV LLLLGAPVML
     MTALMIKLDS PGPILYKQER VGLGGKGFMC IKFRSMRTDA EKDGVARWAS KNDSRITRVG
     AFIRKTRIDE LPQLFSVLRG EMSMVGPRPE RPSFVAQLRE QIPYYDLRHT VKPGLTGWAQ
     VRYAYGASLE DARKKHQFDL YYVKNNSLLL DLQVLIETVS VVLFREGAH
//
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