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Database: UniProt
Entry: A0A1X2LW48_9MYCO
LinkDB: A0A1X2LW48_9MYCO
Original site: A0A1X2LW48_9MYCO 
ID   A0A1X2LW48_9MYCO        Unreviewed;      1067 AA.
AC   A0A1X2LW48;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=MFS transporter {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B8W66_08255 {ECO:0000313|EMBL:OSC41379.1};
OS   Mycobacterium decipiens.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1430326 {ECO:0000313|EMBL:OSC41379.1, ECO:0000313|Proteomes:UP000193247};
RN   [1] {ECO:0000313|EMBL:OSC41379.1, ECO:0000313|Proteomes:UP000193247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TBL 1200985 {ECO:0000313|EMBL:OSC41379.1,
RC   ECO:0000313|Proteomes:UP000193247};
RA   Tortoli E., Trovato A., Cirillo D.M.;
RT   "The new phylogeny of genus Mycobacterium.";
RL   Submitted (APR-2017) 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 NTE family. {ECO:0000256|ARBA:ARBA00006636}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. EmrB family.
CC       {ECO:0000256|ARBA:ARBA00008537}.
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:OSC41379.1}.
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DR   EMBL; NCXP01000007; OSC41379.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2LW48; -.
DR   STRING; 1430326.B8W66_08255; -.
DR   OrthoDB; 7375466at2; -.
DR   Proteomes; UP000193247; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:UniProt.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd17321; MFS_MMR_MDR_like; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   Gene3D; 1.20.1720.10; Multidrug resistance protein D; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR004638; EmrB-like.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   NCBIfam; TIGR00711; efflux_EmrB; 1.
DR   PANTHER; PTHR42718:SF47; DRUG EFFLUX PUMP JEFA; 1.
DR   PANTHER; PTHR42718; MAJOR FACILITATOR SUPERFAMILY MULTIDRUG TRANSPORTER MFSC; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF07690; MFS_1; 2.
DR   Pfam; PF01734; Patatin; 1.
DR   PRINTS; PR01036; TCRTETB.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 2.
DR   PROSITE; PS00889; CNMP_BINDING_2; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS51635; PNPLA; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        82..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        110..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        135..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        169..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        196..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        234..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        256..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        298..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        334..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        360..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        398..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        438..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          44..488
FT                   /note="Major facilitator superfamily (MFS) profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50850"
FT   DOMAIN          523..631
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          808..967
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   REGION          978..998
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1067 AA;  111321 MW;  BB51FA996104F0BF CRC64;
     MPAQTVTANV AASVIDDGPV EPGRWGSRTG VPPARRRQPS SAAVLLVAAF GAFLAFLDST
     IVNVAFPDIQ RHFQSDISDL SWVLNAYNIV FAAFLVASGR LADLLGRKRV FIYGVVLFTV
     ASGLCAIADS VGQLVAFRVL QGIGAAVLVP ASLGLVVEAF PAARRAHGVN LWGAAGAIAA
     GLGPPIGGAL VEADGWRWVF LVNLPLGVLA VLAARRALVE NRASGRRRVP DVRGALLLAI
     ALGFLTLGLI KGPDWGWASL PAIGSLLAAA VAMVGFVMSS RHHPAPMVDP ALLRIRSFVA
     GTGLTAVASA GFYAYLLTHV LFLNYVWGYT LLEAGLAVAP AALVAAVVAA LLGRVADRHG
     YRFIIGIGAL IWAGSLLWYL KVVGSTPDFL GEWLPGQILQ GIGVGATFPL LGSASLARLA
     KGGSYATASA VTGTIRQVGA VVGIALLVIL VGTPAPGAAE EVLRRGWTMA AICFVAVAFG
     AVLLGRIRPV PAATAEAPPA PPVAPLGSQR PMPAPVRPPA APVAPVLKAS RELDLLAALR
     SARPDAQLVE LQAGSYLFHA GDASDALYVV RSGRLLVLAG NGEKEDVVAE LGRGQVVGEL
     GVLLNAPRSA TVRAVRDSSL TRVTKAEFDK IADAGVLGAL AGVLAKRQHQ TRTASQRTTP
     EAVVAVIGVN SNAPVAMVAT ELCAALSTRL RAIAPGRVDR DGLERAEQAA DRVVLHAAAD
     DALWRDFCMR VADRVVLVSS NPAPPSATLP ARATGADLVL AGPPAGREHR RAWEELITPR
     SMHTIRRGHV ADDLRVLATR IAGRSVGLVL SGGAARACAH LGVLEELEAA GVTVDRFAGT
     SMGAIIAALA ASGMDAAGVD AQIYEHFVRK SHGDYTLPRK GLIRGKRTQA ALRTIFGDQL
     VEELPKHFRC VSVDLLGRRP IVHRRGPLAD VVGCSMRLPF LYAPMPYNGT LHVDGGVLDN
     VPVTTLVGKD GPLIAVNVAS GGNPSPTSSG NRRRKPRVPG LTDTLLRTMT ISSAIASESV
     LAQADLVIKP NPTGVGLMEY HQIDLAREAG RNAAREALPQ IMELVHR
//
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