ID   MMPL8_MYCTO             Reviewed;        1089 AA.
AC   P9WJU4; L0TFD0; O07800;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Sulfolipid-1 exporter MmpL8 {ECO:0000250|UniProtKB:P9WJU5};
GN   Name=mmpL8; OrderedLocusNames=MT3931;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Required for the biosynthesis and the transport across the
CC       inner membrane of sulfolipid-1 (SL-1), which is a major cell wall lipid
CC       of pathogenic mycobacteria. Could also transport SL1278 (2-palmitoyl-3-
CC       (C43)-phthioceranyl-alpha, alpha'-D-trehalose-2'-sulfate), which is the
CC       precursor of SL-1. {ECO:0000250|UniProtKB:P9WJU5}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P9WJU5}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the resistance-nodulation-cell division (RND)
CC       (TC 2.A.6) family. MmpL subfamily. {ECO:0000305}.
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DR   EMBL; AE000516; AAK48298.1; -; Genomic_DNA.
DR   PIR; C70522; C70522.
DR   RefSeq; WP_003899710.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WJU4; -.
DR   EnsemblBacteria; AAK48298; AAK48298; MT3931.
DR   KEGG; mtc:MT3931; -.
DR   PATRIC; fig|83331.31.peg.4228; -.
DR   HOGENOM; CLU_005108_3_2_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR004869; MMPL_dom.
DR   InterPro; IPR000731; SSD.
DR   Pfam; PF03176; MMPL; 2.
DR   PROSITE; PS50156; SSD; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Cell wall biogenesis/degradation;
KW   Lipid transport; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1089
FT                   /note="Sulfolipid-1 exporter MmpL8"
FT                   /id="PRO_0000427769"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        400..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        555..575
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        874..894
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        898..918
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        930..950
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        973..993
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        996..1016
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1056..1078
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1089 AA;  115998 MW;  E9F842026831060F CRC64;
     MCDVLMQPVR TPRPSTNLRS KPLRPTGDGG VFPRLGRLIV RRPWVVIAFW VALAGLLAPT
     VPSLDAISQR HPVAILPSDA PVLVSTRQMT AAFREAGLQS VAVVVLSDAK GLGAADERSY
     KELVDALRRD TRDVVMLQDF VTTPPLRELM TSKDNQAWIL PVGLPGDLGS TQSKQAYARV
     ADIVEHQVAG STLTANLTGP AATVADLNLT GQRDRSRIEF AITILLLVIL LIIYGNPITM
     VLPLITIGMS VVVAQRLVAI AGLAGLGIAN QSIIFMSGMM VGAGTDYAVF LISRYHDYLR
     QGADSDQAVK KALTSIGKVI AASAATVAIT FLGMVFTQLG ILKTVGPMLG ISVAVVFFAA
     VTLLPALMVL TGRRGWIAPR RDLTRRFWRS SGVHIVRRPK THLLASALVL VILAGCAGLA
     RYNYDDRKTL PASVESSIGY AALDKHFPSN LIIPEYLFIQ SSTDLRTPKA LADLEQMVQR
     VSQVPGVAMV RGITRPAGRS LEQARTSWQA GEVGSKLDEG SKQIAVHTGD IDKLAGGANL
     MASKLGDVRA QVNRAISTVG GLIDALAYLQ DLLGGNRVLG ELEGAEKLIG SMRALGDTID
     ADASFVANNT EWASPVLGAL DSSPMCTADP ACASARTELQ RLVTARDDGT LAKISELARQ
     LQATRAVQTL AATVSGLRGA LATVIRAMGS LGMSSPGGVR SKINLVNKGV NDLADGSRQL
     AEGVQLLVDQ VKKMGFGLGE ASAFLLAMKD TATTPAMAGF YIPPELLSYA TGESVKAETM
     PSEYRDLLGG LNVDQLKKVA AAFISPDGHS IRYLIQTDLN PFSTAAMDQI DAITAAARGA
     QPNTALADAK VSVVGLPVVL KDTRDYSDHD LRLIIAMTVC IVLLILIVLL RAIVAPLYLI
     GSVIVSYLAA LGIGVIVFQF LLGQEMHWSI PGLTFVILVA VGADYNMLLI SRLREEAVLG
     VRSGVIRTVA STGGVITAAG LIMAASMYGL VFASLGSVVQ GAFVLGTGLL LDTFLVRTVT
     VPAIAVLVGQ ANWWLPSSWR PATWWPLGRR RGRAQRTKRK PLLPKEEEEQ SPPDDDDLIG
     LWLHDGLRL