ID A4T3X2_MYCGI Unreviewed; 1001 AA.
AC A4T3X2;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Transport protein {ECO:0000313|EMBL:ABP42897.1};
GN OrderedLocusNames=Mflv_0403 {ECO:0000313|EMBL:ABP42897.1};
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP42897.1};
RN [1] {ECO:0000313|EMBL:ABP42897.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP42897.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP42897.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP42897.1};
RX PubMed=23469141;
RA Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT during Pyrene Degradation.";
RL PLoS ONE 8:E58066-E58066(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the resistance-nodulation-cell division (RND)
CC (TC 2.A.6) family. MmpL subfamily. {ECO:0000256|ARBA:ARBA00010157}.
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DR EMBL; CP000656; ABP42897.1; -; Genomic_DNA.
DR AlphaFoldDB; A4T3X2; -.
DR STRING; 350054.Mflv_0403; -.
DR KEGG; mgi:Mflv_0403; -.
DR eggNOG; COG2409; Bacteria.
DR HOGENOM; CLU_005108_3_0_11; -.
DR OrthoDB; 2365435at2; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR InterPro; IPR004869; MMPL_dom.
DR InterPro; IPR004707; MmpL_fam.
DR InterPro; IPR000731; SSD.
DR NCBIfam; TIGR00833; actII; 1.
DR PANTHER; PTHR33406; MEMBRANE PROTEIN MJ1562-RELATED; 1.
DR PANTHER; PTHR33406:SF6; MEMBRANE PROTEIN SCO0839-RELATED; 1.
DR Pfam; PF03176; MMPL; 2.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR PROSITE; PS50156; SSD; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 324..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 822..841
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 848..872
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 884..902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 914..935
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 941..962
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 218..345
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
SQ SEQUENCE 1001 AA; 105917 MW; 8C00D4A9B18D2451 CRC64;
MRRLADVVVR WPWAVIGVWI ALAVALPLSF PSLGQMAAKN PLQILPADAP SSVTAQKMAE
AFDEPGSDNL LVVAFINESG LVPEDELTYR NVVDALRDDV ADVVSVQDFL GTPQLRQFLT
SEDKTTWVLP VSLVGELGTP RAYESFNRVA DVIRHEVPDA GTGGSSLTVH VTGPAATVAD
LTVAGEQDRL PIEIAIAVLV LGVLLLVYRN PVTMLLPLLT IGASVLIAQG VVAGYSELTG
AGVSNQSIVF LSAILAGAGT DYAVFLISRY HDYLRRGAEA GEAVRAAMAS IGKVITASAS
TVGITFLAMS FAEMGVFRTI GVSAAIGIGV AYLAGVTLLP AILVLAGPRG WIKPRRELTA
QFWRRSGIRI VRRPVPHLVA SALVLALLAG FAIVADFNYD DRKAVDAAAP SSVGYAALER
HFPISQSIPQ YILIQSPKDL RNPQALADLE QMASRIAQLP DVSLVSGVTR PLGEVPAEFR
ATFQAGIVGD RLAAGSAQIG ERSGDLTTLA DGATTLADSL GDVRSQVNEI APSLKGIIDT
FSSVRTEYGG DKLVRDVATA AKLVDSVNKL GLSMGINFRA VRDMFAWIGP VLTALQGNRV
CDANPSCVDT RMQFEKLVSA REDGRVDEIN QLAGQLQGVD DRQSLTATVN QLNGALAQVT
KAISAMGLDT PAGARAGLDD LQDGADRLAD GSRQVAGGVD QLVEQIKVMA AGLDQAAAFL
LTMRNDASSS NMAGFSIPAE VLGAVEFQKA SEAFVSPDGH SVRYLVQTKL NPFSSEAMDQ
VNTISDIARG AQPNTMLSDA SISMGGFPAA LRDTRDYYER DIRFIIVVTL VIVMLVLMLL
LRSLIAPLYL VGSVVVSYFA AIGIGVLVFQ LLLGQQLHWS VPPLAFVVLV AVGADYNMLF
VSRMRDESPH SVRFGIIRTL GSTGGVITAA GLIFAASMAG LLFSSIGIVV QGGFVIGVGI
LLDTFVVRTI TVPAIATLLG RANWWPSRVA APARERVSAD T
//
