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Database: UniProt
Entry: A0A1S2HWP8_9MICO
LinkDB: A0A1S2HWP8_9MICO
Original site: A0A1S2HWP8_9MICO 
ID   A0A1S2HWP8_9MICO        Unreviewed;       588 AA.
AC   A0A1S2HWP8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Choline transporter {ECO:0000313|EMBL:OII15388.1};
GN   ORFNames=BIU97_14545 {ECO:0000313|EMBL:OII15388.1};
OS   Curtobacterium sp. MCBA15_009.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Curtobacterium.
OX   NCBI_TaxID=1898737 {ECO:0000313|EMBL:OII15388.1, ECO:0000313|Proteomes:UP000180289};
RN   [1] {ECO:0000313|EMBL:OII15388.1, ECO:0000313|Proteomes:UP000180289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCBA15_009 {ECO:0000313|EMBL:OII15388.1,
RC   ECO:0000313|Proteomes:UP000180289};
RA   Chase A.B., Arevalo P., Polz M.F., Berlemont R., Martiny J.B.;
RT   "Evidence for ecological flexibility in the cosmopolitan genus
RT   Curtobacterium.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the BCCT transporter (TC 2.A.15) family.
CC       {ECO:0000256|ARBA:ARBA00005658}.
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:OII15388.1}.
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DR   EMBL; MJGO01000003; OII15388.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S2HWP8; -.
DR   OrthoDB; 9775735at2; -.
DR   Proteomes; UP000180289; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0071705; P:nitrogen compound transport; IEA:InterPro.
DR   InterPro; IPR000060; BCCT_transptr.
DR   NCBIfam; TIGR00842; bcct; 1.
DR   PANTHER; PTHR30047:SF7; HIGH-AFFINITY CHOLINE TRANSPORT PROTEIN; 1.
DR   PANTHER; PTHR30047; HIGH-AFFINITY CHOLINE TRANSPORT PROTEIN-RELATED; 1.
DR   Pfam; PF02028; BCCT; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000180289};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        39..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        128..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        178..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        216..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        309..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        338..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        391..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        433..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        462..485
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          545..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..588
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   588 AA;  62416 MW;  79741A3C74BCD47E CRC64;
     MFWPAAVLVL GFVAFTLVSP SSAEAMFVGL QDGIVRNFSW YYVLIAAFFV GFSLFVGFSR
     FGDVKLGKDA DEPEFSTASW FSLLFAAGMG IGLVFYGVSE PLSHFASPRP GVTGDENELA
     QQALVQTFLH WGLHAWAIYV VLGLALAYAI HRRGRPVSIR WALEPLLGQR VRGGWGNLID
     VLALVGTLFG VATSLGLGVI QIGAGLEAAG IAESSIVSQI AIIAVITAVT IVSLVTGVSK
     GMKVLSNFNL LLAAALLLFV LIVGPTQFLL RDFVQSIGAY LQNVVGLSFN VTAQQGAAGE
     EWQGAWTTFY WGWWMSWAPF VGVFIARISK GRTVRQFVFG VLLVPTALTF LWFAVLGGSA
     IHRQTDGAGG LVGADGTVDV EGSLFALLGD LPAGAVLTIG AILLIGVFFV TSSDSGALVM
     AMISSGGDIE PRNWLRVFFA FVSALLAVAL LLSGGLDALK TAAITTALPF SVVLLLTCWS
     TIIAFTRERR AYDKAEREVL LEHVGAYYGL EVEEPTERGG RGGPGAGGLG GLTRPWAAVK
     RRVRGARPGA PEAPVAADAV EDFPVRTEHV SEDPALDAAL DRTGDDDR
//
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