ID I3TIU9_TISMK Unreviewed; 421 AA.
AC I3TIU9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=MFS-type transporter ybfB {ECO:0000313|EMBL:AFK52687.1};
GN Name=ybfB {ECO:0000313|EMBL:AFK52687.1};
GN OrderedLocusNames=TMO_0848 {ECO:0000313|EMBL:AFK52687.1};
OS Tistrella mobilis (strain KA081020-065).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK52687.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK52687.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK52687.1,
RC ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP003236; AFK52687.1; -; Genomic_DNA.
DR RefSeq; WP_014744366.1; NC_017956.1.
DR AlphaFoldDB; I3TIU9; -.
DR STRING; 1110502.TMO_0848; -.
DR KEGG; tmo:TMO_0848; -.
DR eggNOG; COG2271; Bacteria.
DR HOGENOM; CLU_044455_0_0_5; -.
DR Proteomes; UP000005258; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR PANTHER; PTHR11360:SF290; MAJOR FACILITATOR SUPERFAMILY TRANSPORTER; 1.
DR PANTHER; PTHR11360; MONOCARBOXYLATE TRANSPORTER; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005258};
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..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..409
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
SQ SEQUENCE 421 AA; 42439 MW; 9B6D995DF85E23D6 CRC64;
MSAASPLPRQ PGFGLAAWTV VIIGFLSLGL AFSTRAALGL AMPVWEQAEG WSRTEVSNAG
ALALVVMALL APTAGLLTDS HGPRRLLGAG LVMVAAAAGL ISLADGPVML ILAFSVVGGI
GFGAVATHVV ATAVALMVPA ARRGFATGIA TAGATAGQLA LVPILSVWMT ADDWRTGFIG
LALAAGVAAV AALVLLPRAR AAAAVPGGAA PAAEPMGRRI GFLATNPVFH ALFWSFFICG
ITTSGVIEVH LMPYAALCGF PPLPSATAYG VLCAVNLGGM ILAGHLGDRI DRGRLLAVIY
AGRAAALVLL VFIGDDYGLL LIFAVLFGLF DYSTVAPTAG LVADRLGLHR MGLAMGLLSA
GHSLGAALGA WAGGRIFAAT GDYAGLWYGA AALSGVAVLI VLTLARPRGR DLRPGRAALP
A
//
