ID A0A1F4BJD7_9PROT Unreviewed; 528 AA.
AC A0A1F4BJD7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Multidrug MFS transporter {ECO:0000313|EMBL:OGA24461.1};
DE Flags: Fragment;
GN ORFNames=A3I02_05985 {ECO:0000313|EMBL:OGA24461.1};
OS Betaproteobacteria bacterium RIFCSPLOWO2_02_FULL_67_26.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1797492 {ECO:0000313|EMBL:OGA24461.1, ECO:0000313|Proteomes:UP000178840};
RN [1] {ECO:0000313|EMBL:OGA24461.1, ECO:0000313|Proteomes:UP000178840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC {ECO:0000256|ARBA:ARBA00007430}.
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:OGA24461.1}.
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DR EMBL; MERD01000045; OGA24461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4BJD7; -.
DR STRING; 1797492.A3I02_05985; -.
DR Proteomes; UP000178840; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd05237; UDP_invert_4-6DH_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003869; Polysac_CapD-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43318:SF1; POLYSACCHARIDE BIOSYNTHESIS PROTEIN EPSC-RELATED; 1.
DR PANTHER; PTHR43318; UDP-N-ACETYLGLUCOSAMINE 4,6-DEHYDRATASE; 1.
DR Pfam; PF13727; CoA_binding_3; 1.
DR Pfam; PF02719; Polysacc_synt_2; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 279..525
FT /note="Polysaccharide biosynthesis protein CapD-like"
FT /evidence="ECO:0000259|Pfam:PF02719"
FT NON_TER 528
FT /evidence="ECO:0000313|EMBL:OGA24461.1"
SQ SEQUENCE 528 AA; 57634 MW; 3462744835789174 CRC64;
MLRVLLVFAH DLAAAAAAWC LAYALRFNLE ISRAYLEGML QTLPWVIALQ ALVFWRFGLY
RGVWRYASLP DLKRILFAIG VGAMGTALLL HLLLMGDLVP RSVLLLDPIL LLLIMGGSRL
AYRAWKEHRL YGPAQYHGKP VLVLGAGDAA VTLLKDLERS LEWRVVGLLD DDPARQRSLI
LGVRVLGPLD TLAKWAGEMG IDHAIIAMPS ASHTVRRRAT NLCSAAGLQV LTVPSFDDLV
SGKVTVSSIR RVELDDLLGR DPVELDNEGL HQLLADKAVL VTGAGGSIGS ELCRQIARFR
PRRLILFELN EFALYGIEQE FAERFPGLSV VAAIGDAKDV ARVAQIFSQH GPEVVFHAAA
YKHVPLMEED NAWEAVRNNV IGTSVLAEAA ARGGAHKFIL VSTDKAVNPA NVMGASKRLA
ELVCQSLQQS GATQFVIVRF GNVLGSTGSV IPRFREQIAR GGPVTVTHPE ITRYFMSIEE
AAQLVLQAGL MGKGGEIFVL DMGEPVRIVD LARELIRLSG FAEDEIRI
//
