MMPL3_MYCTO
ID MMPL3_MYCTO Reviewed; 944 AA.
AC P9WJV4; L0T2U3; O53657;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Trehalose monomycolate exporter MmpL3 {ECO:0000250|UniProtKB:P9WJV5};
DE Short=TMM exporter MmpL3 {ECO:0000250|UniProtKB:P9WJV5};
DE AltName: Full=MmpL3 transporter {ECO:0000305};
DE AltName: Full=Mycobacterial membrane protein large 3 {ECO:0000305};
GN Name=mmpL3; OrderedLocusNames=MT0216;
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: Transports trehalose monomycolate (TMM) to the cell wall.
CC Flips TMM across the inner membrane. Membrane potential is not required
CC for this function. Transports probably phosphatidylethanolamine (PE) as
CC well. Binds specifically both TMM and PE, but not trehalose dimycolate
CC (TDM). Binds also diacylglycerol (DAG) and other phospholipids,
CC including phosphatidylglycerol (PG), phosphatidylinositol (PI), and
CC cardiolipin (CDL). Contributes to membrane potential, cell wall
CC composition, antibiotic susceptibility and fitness (By similarity).
CC Could also be part of a heme-iron acquisition system (By similarity).
CC {ECO:0000250|UniProtKB:A0QP27, ECO:0000250|UniProtKB:P9WJV5}.
CC -!- SUBUNIT: Monomer. Interacts with TtfA (via N-terminus); active
CC trehalose monomycolate (TMM) biosynthesis is not required for the
CC complex formation. {ECO:0000250|UniProtKB:A0QP27}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P9WJV5}; Multi-pass membrane protein
CC {ECO:0000255}. Cell septum {ECO:0000250|UniProtKB:A0QP27}. Cell tip
CC {ECO:0000250|UniProtKB:A0QP27}. Note=Colocalizes with TtfA to the cell
CC poles and septa. Trehalose monomycolate (TMM) synthesis is not required
CC for localization to the poles or septa. {ECO:0000250|UniProtKB:A0QP27}.
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; AAK44437.1; -; Genomic_DNA.
DR PIR; C70839; C70839.
DR AlphaFoldDB; P9WJV4; -.
DR SMR; P9WJV4; -.
DR EnsemblBacteria; AAK44437; AAK44437; MT0216.
DR KEGG; mtc:MT0216; -.
DR HOGENOM; CLU_005108_8_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0030428; C:cell septum; ISS:UniProtKB.
DR GO; GO:0051286; C:cell tip; ISS:UniProtKB.
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:1901612; F:cardiolipin binding; ISS:UniProtKB.
DR GO; GO:0019992; F:diacylglycerol binding; ISS:UniProtKB.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; ISS:UniProtKB.
DR GO; GO:1901611; F:phosphatidylglycerol binding; ISS:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0042546; P:cell wall biogenesis; ISS:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0071768; P:mycolic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; ISS:UniProtKB.
DR GO; GO:0046677; P:response to antibiotic; ISS:UniProtKB.
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..944
FT /note="Trehalose monomycolate exporter MmpL3"
FT /id="PRO_0000427764"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..185
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..235
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27, ECO:0000305"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..314
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..562
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 563..583
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 584..586
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 587..607
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 608..616
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 617..637
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 638..672
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 673..693
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 694..698
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 699..719
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 720..944
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT REGION 778..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40..44
FT /ligand="1,2-diacylglycero-3-phosphoethanolamine"
FT /ligand_id="ChEBI:CHEBI:57613"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT SITE 251
FT /note="Part of the proton-transportation channel"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT SITE 252
FT /note="Part of the proton-transportation channel"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT SITE 586
FT /note="Part of the proton transportation network"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT SITE 640
FT /note="Part of the proton-transportation channel"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT SITE 641
FT /note="Part of the proton-transportation channel"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT SITE 642
FT /note="Part of the proton transportation network"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
SQ SEQUENCE 944 AA; 100890 MW; 69BB883DBFCB4B7A CRC64;
MFAWWGRTVY RYRFIVIGVM VALCLGGGVF GLSLGKHVTQ SGFYDDGSQS VQASVLGDQV
YGRDRSGHIV AIFQAPAGKT VDDPAWSKKV VDELNRFQQD HPDQVLGWAG YLRASQATGM
ATADKKYTFV SIPLKGDDDD TILNNYKAIA PDLQRLDGGT VKLAGLQPVA EALTGTIATD
QRRMEVLALP LVAVVLFFVF GGVIAAGLPV MVGGLCIAGA LGIMRFLAIF GPVHYFAQPV
VSLIGLGIAI DYGLFIVSRF REEIAEGYDT ETAVRRTVIT AGRTVTFSAV LIVASAIGLL
LFPQGFLKSL TYATIASVML SAILSITVLP ACLGILGKHV DALGVRTLFR VPFLANWKIS
AAYLNWLADR LQRTKTREEV EAGFWGKLVN RVMKRPVLFA APIVIIMILL IIPVGKLSLG
GISEKYLPPT NSVRQAQEEF DKLFPGYRTN PLTLVIQTSN HQPVTDAQIA DIRSKAMAIG
GFIEPDNDPA NMWQERAYAV GASKDPSVRV LQNGLINPAD ASKKLTELRA ITPPKGITVL
VGGTPALELD SIHGLFAKMP LMVVILLTTT IVLMFLAFGS VVLPIKATLM SALTLGSTMG
ILTWIFVDGH FSKWLNFTPT PLTAPVIGLI IALVFGLSTD YEVFLVSRMV EARERGMSTQ
EAIRIGTAAT GRIITAAALI VAVVAGAFVF SDLVMMKYLA FGLMAALLLD ATVVRMFLVP
SVMKLLGDDC WWAPRWARRL QTRIGLGEIH LPDERNRPVS NGRPARPPVT AGLVAARAAG
DPRPPHDPTH PLAESPRPAR SSPASSPELT PALEATAAPA APSGASTTRM QIGSSTEPPT
TRLAAAGRSV QSPASTPPPT PTPPSAPSAG QTRAMPLAAN RSTDAAGDPA EPTAALPIIR
SDGDDSEAAT EQLNARGTSD KTRQRRRGGG ALSAQDLLRR EGRL
