MMPL3_MYCLE
ID MMPL3_MYCLE Reviewed; 955 AA.
AC O06081;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable 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=ML2620; ORFNames=MLCL622.18c;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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. Contributes to membrane potential, cell wall composition,
CC antibiotic susceptibility and fitness. {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}.
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; Z95398; CAB08813.1; -; Genomic_DNA.
DR EMBL; AL583926; CAC32152.1; -; Genomic_DNA.
DR PIR; B87237; B87237.
DR RefSeq; NP_302678.1; NC_002677.1.
DR RefSeq; WP_010908997.1; NC_002677.1.
DR AlphaFoldDB; O06081; -.
DR SMR; O06081; -.
DR STRING; 272631.ML2620; -.
DR EnsemblBacteria; CAC32152; CAC32152; CAC32152.
DR KEGG; mle:ML2620; -.
DR PATRIC; fig|272631.5.peg.5021; -.
DR Leproma; ML2620; -.
DR eggNOG; COG2409; Bacteria.
DR HOGENOM; CLU_005108_8_0_11; -.
DR OMA; SRAYLNW; -.
DR Proteomes; UP000000806; 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:0008429; F:phosphatidylethanolamine 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 Pfam; PF03176; MMPL; 2.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cell wall biogenesis/degradation;
KW Lipid transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..955
FT /note="Probable trehalose monomycolate exporter MmpL3"
FT /id="PRO_0000103565"
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..190
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 191..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 220..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..244
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 245..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..319
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..567
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 568..588
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 589..591
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 592..612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 613..621
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..678
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 700..703
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT TRANSMEM 704..724
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 725..955
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT REGION 759..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..939
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 256
FT /note="Part of the proton-transportation channel"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT SITE 257
FT /note="Part of the proton-transportation channel"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT SITE 591
FT /note="Part of the proton transportation network"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT SITE 645
FT /note="Part of the proton-transportation channel"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT SITE 646
FT /note="Part of the proton-transportation channel"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
FT SITE 647
FT /note="Part of the proton transportation network"
FT /evidence="ECO:0000250|UniProtKB:A0QP27"
SQ SEQUENCE 955 AA; 102792 MW; 8AF86562EB91D07B CRC64;
MFAWWGRTVY RYRFIVIGIT VALCLCGGVF GLSLGKHVTQ SGFYDDSSQS VKASILGDQV
YGRDRSGHIV AIFHAPDGKT VNDPAWAKKI TDELNQFQRN NSNKVTGWAG YLRASDTTNT
VVQGMATPDK KYTFVSIPLK GDDDDTILNN YKAIAPDLQK LDGGTVQLAG LDPIANALTS
TIATDQRRME VLALPLVAVV LFLVFGGVIA ACLPVMVGGL SIAGALGILR FIALFGPVHF
FAQPVVSLIG LGIAVDYGLF VVSRFREEIA EGYDTEAAVR RTVMTAGRTV TFSAVLIAAS
GASLLLLPQG FVKSLTYALI AAVTLAALLS ITLLPACLAI LAKHVDALGV RTLFRVPLLR
NWRMSHACLN WLADRLQKTK TREEVEAGFW GKLVNFVMKR PLVFAIPIVI GMILLVIPLG
NLSFGGMSEK YLPPNNAVRQ SQEHFDQLFP GYRTNPLTLV IQTSNHQPVT DQEIADIRSK
AMAISGFIEP DNNYVNMWQE RTVAPGASKD PSVRVLQNGL INPNDASKKI NELRSITPPK
GLTVSVGGTP ALEQDSIHSL VAQAPLMVIM LITTTMLLMF LAFGSFVLPI KAAVMSALTL
GSTMGILTWI FVDGHLSKWL NFTPTPLMVV IIALVVAVGY GLATDYEVFL VSRMVEARAE
SMSTQEAVRI GTASTGRLIT AAALVLAVVA GSFVFSDLVM MKYLAFGLMA ALLLDATVVR
MFLVPSVMKL LGDDCWWAPR WARLLQNRIG LGEIHLPDER RRPTVSGRPV RPPVTAASLA
APASRVPRGP THPATLEPSQ RARSGLASRP QIKRPQELPS GASTARIQMR PSQSVEATTT
RLSVPGNAPT TAAVSSSQGV QAVPLAATRH PLPTPSPASG QTRAMPVPAN RSSDNASETA
EPTTALPIMR PQDNDSEVAT EKLNALGQGD NSRQHRRATG GGISAQDLLR REGRL
