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Trehalose monomycolate exporter MmpL3 (TMM exporter MmpL3)

 MMPL3_MYCTU             Reviewed;         944 AA.
P9WJV5; L0T2U3; O53657;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
07-JUN-2017, entry version 20.
RecName: Full=Trehalose monomycolate exporter MmpL3 {ECO:0000305};
Short=TMM exporter MmpL3 {ECO:0000305};
Name=mmpL3; OrderedLocusNames=Rv0206c;
ORFNames=MTCY08D5.01c, MTV033.14c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[3]
PUTATIVE FUNCTION IN HEME IMPORT, AND HEME BINDING.
PubMed=21383189; DOI=10.1073/pnas.1009516108;
Tullius M.V., Harmston C.A., Owens C.P., Chim N., Morse R.P.,
McMath L.M., Iniguez A., Kimmey J.M., Sawaya M.R., Whitelegge J.P.,
Horwitz M.A., Goulding C.W.;
"Discovery and characterization of a unique mycobacterial heme
acquisition system.";
Proc. Natl. Acad. Sci. U.S.A. 108:5051-5056(2011).
[4]
ENZYME REGULATION, AND MUTAGENESIS OF VAL-51; LEU-320; THR-667 AND
VAL-684.
PubMed=22577943; DOI=10.1021/cb300151m;
Stanley S.A., Grant S.S., Kawate T., Iwase N., Shimizu M., Wivagg C.,
Silvis M., Kazyanskaya E., Aquadro J., Golas A., Fitzgerald M.,
Dai H., Zhang L., Hung D.T.;
"Identification of novel inhibitors of M. tuberculosis growth using
whole cell based high-throughput screening.";
ACS Chem. Biol. 7:1377-1384(2012).
[5]
ENZYME REGULATION, AND MUTAGENESIS OF LEU-215.
STRAIN=H37Rv;
PubMed=22024828; DOI=10.1128/AAC.05270-11;
La Rosa V., Poce G., Canseco J.O., Buroni S., Pasca M.R., Biava M.,
Raju R.M., Porretta G.C., Alfonso S., Battilocchio C., Javid B.,
Sorrentino F., Ioerger T.R., Sacchettini J.C., Manetti F., Botta M.,
De Logu A., Rubin E.J., De Rossi E.;
"MmpL3 is the cellular target of the antitubercular pyrrole derivative
BM212.";
Antimicrob. Agents Chemother. 56:324-331(2012).
[6]
FUNCTION, IDENTIFICATION AS A DRUG TARGET, ENZYME REGULATION, AND
MUTAGENESIS OF GLN-40; LEU-567 AND ALA-700.
STRAIN=H37Rv;
PubMed=22252828; DOI=10.1128/AAC.05708-11;
Tahlan K., Wilson R., Kastrinsky D.B., Arora K., Nair V., Fischer E.,
Barnes S.W., Walker J.R., Alland D., Barry C.E. III, Boshoff H.I.;
"SQ109 targets MmpL3, a membrane transporter of trehalose monomycolate
involved in mycolic acid donation to the cell wall core of
Mycobacterium tuberculosis.";
Antimicrob. Agents Chemother. 56:1797-1809(2012).
[7]
FUNCTION, ENZYME REGULATION, AND MUTAGENESIS OF GLY-253.
STRAIN=H37Rv;
PubMed=22344175; DOI=10.1038/nchembio.794;
Grzegorzewicz A.E., Pham H., Gundi V.A., Scherman M.S., North E.J.,
Hess T., Jones V., Gruppo V., Born S.E., Kordulakova J., Chavadi S.S.,
Morisseau C., Lenaerts A.J., Lee R.E., McNeil M.R., Jackson M.;
"Inhibition of mycolic acid transport across the Mycobacterium
tuberculosis plasma membrane.";
Nat. Chem. Biol. 8:334-341(2012).
[8]
ENZYME REGULATION, AND MUTAGENESIS OF SER-288.
PubMed=24352433; DOI=10.1038/ncomms3907;
Lun S., Guo H., Onajole O.K., Pieroni M., Gunosewoyo H., Chen G.,
Tipparaju S.K., Ammerman N.C., Kozikowski A.P., Bishai W.R.;
"Indoleamides are active against drug-resistant Mycobacterium
tuberculosis.";
Nat. Commun. 4:2907-2907(2013).
[9]
ENZYME REGULATION.
PubMed=23613759; DOI=10.1371/journal.pone.0060933;
Remuinan M.J., Perez-Herran E., Rullas J., Alemparte C.,
Martinez-Hoyos M., Dow D.J., Afari J., Mehta N., Esquivias J.,
Jimenez E., Ortega-Muro F., Fraile-Gabaldon M.T., Spivey V.L.,
Loman N.J., Pallen M.J., Constantinidou C., Minick D.J., Cacho M.,
Rebollo-Lopez M.J., Gonzalez C., Sousa V., Angulo-Barturen I.,
Mendoza-Losana A., Barros D., Besra G.S., Ballell L., Cammack N.;
"Tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide and N-benzyl-6',7'-
dihydrospiro[piperidine-4,4'-thieno[3,2-c]pyran] analogues with
bactericidal efficacy against Mycobacterium tuberculosis targeting
MmpL3.";
PLoS ONE 8:E60933-E60933(2013).
[10]
ENZYME REGULATION, AND MECHANISM OF INHIBITION.
PubMed=25136022; DOI=10.1128/AAC.03229-14;
Li W., Upadhyay A., Fontes F.L., North E.J., Wang Y., Crans D.C.,
Grzegorzewicz A.E., Jones V., Franzblau S.G., Lee R.E., Crick D.C.,
Jackson M.;
"Novel insights into the mechanism of inhibition of MmpL3, a target of
multiple pharmacophores in Mycobacterium tuberculosis.";
Antimicrob. Agents Chemother. 58:6413-6423(2014).
[11]
REVIEW.
PubMed=24325728; DOI=10.1517/14728222.2014.859677;
Rayasam G.V.;
"MmpL3 a potential new target for development of novel anti-
tuberculosis drugs.";
Expert Opin. Ther. Targets 18:247-256(2014).
-!- FUNCTION: Transports trehalose monomycolate (TMM) across the inner
membrane (PubMed:22252828, PubMed:22344175). Could also be part of
a heme-iron acquisition system (PubMed:21383189).
{ECO:0000269|PubMed:22252828, ECO:0000269|PubMed:22344175,
ECO:0000305|PubMed:21383189}.
-!- FUNCTION: Is the target of the antitubercular drug SQ109.
{ECO:0000269|PubMed:22252828}.
-!- ENZYME REGULATION: Inhibited by the antitubercular drug SQ109.
Also inhibited by several other compounds such as the pyrrole
derivative BM212, the adamantyl urea derivative AU1235, the
benzimidazole C215, indoleamides, tetrahydropyrazolo[1,5-
a]pyrimidine-3-carboxamide (THPP) and N-benzyl-6',7'-
dihydrospiro[piperidine-4,4'-thieno[3,2-c]pyran] (Spiro) analogs.
Inhibitory effects of these compounds, including SQ109, are most
likely due to their ability to dissipate the transmembrane
electrochemical proton gradient. {ECO:0000269|PubMed:22024828,
ECO:0000269|PubMed:22252828, ECO:0000269|PubMed:22344175,
ECO:0000269|PubMed:22577943, ECO:0000269|PubMed:23613759,
ECO:0000269|PubMed:24352433, ECO:0000269|PubMed:25136022}.
-!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-
pass membrane protein {ECO:0000255}.
-!- SIMILARITY: Belongs to the resistance-nodulation-cell division
(RND) (TC 2.A.6) family. MmpL subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AL123456; CCP42934.1; -; Genomic_DNA.
PIR; C70839; C70839.
RefSeq; NP_214720.1; NC_000962.3.
RefSeq; WP_003899855.1; NZ_KK339370.1.
ProteinModelPortal; P9WJV5; -.
STRING; 83332.Rv0206c; -.
PaxDb; P9WJV5; -.
EnsemblBacteria; CCP42934; CCP42934; Rv0206c.
GeneID; 886752; -.
KEGG; mtu:Rv0206c; -.
TubercuList; Rv0206c; -.
eggNOG; ENOG4107R13; Bacteria.
eggNOG; COG2409; LUCA.
KO; K20470; -.
OMA; TWIFIDG; -.
PhylomeDB; P9WJV5; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005576; C:extracellular region; IGI:MTBBASE.
GO; GO:0005887; C:integral component of plasma membrane; IDA:MTBBASE.
GO; GO:0071766; P:Actinobacterium-type cell wall biogenesis; IDA:MTBBASE.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0040007; P:growth; IDA:MTBBASE.
GO; GO:0015920; P:lipopolysaccharide transport; IDA:MTBBASE.
InterPro; IPR004869; MMPL_dom.
InterPro; IPR000731; SSD.
Pfam; PF03176; MMPL; 2.
PROSITE; PS50156; SSD; 1.
1: Evidence at protein level;
Cell inner membrane; Cell membrane; Cell wall biogenesis/degradation;
Complete proteome; Lipid transport; Membrane; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 944 Trehalose monomycolate exporter MmpL3.
/FTId=PRO_0000103564.
TRANSMEM 14 34 Helical. {ECO:0000255}.
TRANSMEM 186 206 Helical. {ECO:0000255}.
TRANSMEM 210 230 Helical. {ECO:0000255}.
TRANSMEM 236 256 Helical. {ECO:0000255}.
TRANSMEM 287 307 Helical. {ECO:0000255}.
TRANSMEM 315 335 Helical. {ECO:0000255}.
TRANSMEM 397 417 Helical. {ECO:0000255}.
TRANSMEM 563 583 Helical. {ECO:0000255}.
TRANSMEM 587 607 Helical. {ECO:0000255}.
TRANSMEM 617 637 Helical. {ECO:0000255}.
TRANSMEM 673 693 Helical. {ECO:0000255}.
TRANSMEM 699 719 Helical. {ECO:0000255}.
MUTAGEN 40 40 Q->R: Confers resistance to SQ109.
{ECO:0000269|PubMed:22252828}.
MUTAGEN 51 51 V->A: Confers resistance to C215.
{ECO:0000269|PubMed:22577943}.
MUTAGEN 215 215 L->S: Confers resistance to BM212.
{ECO:0000269|PubMed:22024828}.
MUTAGEN 253 253 G->E: Increases resistance to AU1235.
{ECO:0000269|PubMed:22344175}.
MUTAGEN 288 288 S->T: Confers resistance to indoleamides.
{ECO:0000269|PubMed:24352433}.
MUTAGEN 320 320 L->P: Confers resistance to C215.
{ECO:0000269|PubMed:22577943}.
MUTAGEN 567 567 L->P: Confers resistance to SQ109.
{ECO:0000269|PubMed:22252828}.
MUTAGEN 667 667 T->A: Confers resistance to C215.
{ECO:0000269|PubMed:22577943}.
MUTAGEN 684 684 V->A: Confers resistance to C215.
{ECO:0000269|PubMed:22577943}.
MUTAGEN 700 700 A->T: Confers resistance to SQ109.
{ECO:0000269|PubMed:22252828}.
SEQUENCE 944 AA; 100904 MW; 2B9DF83ACDBE490D 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 LPDERKRPVS NGRPARPPVT AGLVAARAAG
DPRPPHDPTH PLAESPRPAR SSPASSPELT PALEATAAPA APSGASTTRM QIGSSTEPPT
TRLAAAGRSV QSPASTPPPT PTPPSAPSAG QTRAMPLAAN RSTDAAGDPA EPTAALPIIR
SDGDDSEAAT EQLNARGTSD KTRQRRRGGG ALSAQDLLRR EGRL


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