MMPL3_MYCTU
ID MMPL3_MYCTU Reviewed; 944 AA.
AC P9WJV5; 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:0000305};
DE Short=TMM exporter MmpL3 {ECO:0000305};
DE AltName: Full=MmpL3 transporter {ECO:0000305};
DE AltName: Full=Mycobacterial membrane protein large 3 {ECO:0000305};
GN Name=mmpL3; OrderedLocusNames=Rv0206c; ORFNames=MTCY08D5.01c, MTV033.14c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP PUTATIVE FUNCTION IN HEME IMPORT, AND HEME BINDING.
RX PubMed=21383189; DOI=10.1073/pnas.1009516108;
RA Tullius M.V., Harmston C.A., Owens C.P., Chim N., Morse R.P., McMath L.M.,
RA Iniguez A., Kimmey J.M., Sawaya M.R., Whitelegge J.P., Horwitz M.A.,
RA Goulding C.W.;
RT "Discovery and characterization of a unique mycobacterial heme acquisition
RT system.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:5051-5056(2011).
RN [4]
RP ACTIVITY REGULATION, AND MUTAGENESIS OF VAL-51; LEU-320; THR-667 AND
RP VAL-684.
RX PubMed=22577943; DOI=10.1021/cb300151m;
RA Stanley S.A., Grant S.S., Kawate T., Iwase N., Shimizu M., Wivagg C.,
RA Silvis M., Kazyanskaya E., Aquadro J., Golas A., Fitzgerald M., Dai H.,
RA Zhang L., Hung D.T.;
RT "Identification of novel inhibitors of M. tuberculosis growth using whole
RT cell based high-throughput screening.";
RL ACS Chem. Biol. 7:1377-1384(2012).
RN [5]
RP ACTIVITY REGULATION, AND MUTAGENESIS OF LEU-215.
RC STRAIN=H37Rv;
RX PubMed=22024828; DOI=10.1128/aac.05270-11;
RA La Rosa V., Poce G., Canseco J.O., Buroni S., Pasca M.R., Biava M.,
RA Raju R.M., Porretta G.C., Alfonso S., Battilocchio C., Javid B.,
RA Sorrentino F., Ioerger T.R., Sacchettini J.C., Manetti F., Botta M.,
RA De Logu A., Rubin E.J., De Rossi E.;
RT "MmpL3 is the cellular target of the antitubercular pyrrole derivative
RT BM212.";
RL Antimicrob. Agents Chemother. 56:324-331(2012).
RN [6]
RP FUNCTION, IDENTIFICATION AS A DRUG TARGET, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF GLN-40; LEU-567 AND ALA-700.
RC STRAIN=H37Rv;
RX PubMed=22252828; DOI=10.1128/aac.05708-11;
RA Tahlan K., Wilson R., Kastrinsky D.B., Arora K., Nair V., Fischer E.,
RA Barnes S.W., Walker J.R., Alland D., Barry C.E. III, Boshoff H.I.;
RT "SQ109 targets MmpL3, a membrane transporter of trehalose monomycolate
RT involved in mycolic acid donation to the cell wall core of Mycobacterium
RT tuberculosis.";
RL Antimicrob. Agents Chemother. 56:1797-1809(2012).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF GLY-253.
RC STRAIN=H37Rv;
RX PubMed=22344175; DOI=10.1038/nchembio.794;
RA Grzegorzewicz A.E., Pham H., Gundi V.A., Scherman M.S., North E.J.,
RA Hess T., Jones V., Gruppo V., Born S.E., Kordulakova J., Chavadi S.S.,
RA Morisseau C., Lenaerts A.J., Lee R.E., McNeil M.R., Jackson M.;
RT "Inhibition of mycolic acid transport across the Mycobacterium tuberculosis
RT plasma membrane.";
RL Nat. Chem. Biol. 8:334-341(2012).
RN [8]
RP ACTIVITY REGULATION, AND MUTAGENESIS OF SER-288.
RX PubMed=24352433; DOI=10.1038/ncomms3907;
RA Lun S., Guo H., Onajole O.K., Pieroni M., Gunosewoyo H., Chen G.,
RA Tipparaju S.K., Ammerman N.C., Kozikowski A.P., Bishai W.R.;
RT "Indoleamides are active against drug-resistant Mycobacterium
RT tuberculosis.";
RL Nat. Commun. 4:2907-2907(2013).
RN [9]
RP ACTIVITY REGULATION.
RX PubMed=23613759; DOI=10.1371/journal.pone.0060933;
RA Remuinan M.J., Perez-Herran E., Rullas J., Alemparte C., Martinez-Hoyos M.,
RA Dow D.J., Afari J., Mehta N., Esquivias J., Jimenez E., Ortega-Muro F.,
RA Fraile-Gabaldon M.T., Spivey V.L., Loman N.J., Pallen M.J.,
RA Constantinidou C., Minick D.J., Cacho M., Rebollo-Lopez M.J., Gonzalez C.,
RA Sousa V., Angulo-Barturen I., Mendoza-Losana A., Barros D., Besra G.S.,
RA Ballell L., Cammack N.;
RT "Tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide and N-benzyl-6',7'-
RT dihydrospiro[piperidine-4,4'-thieno[3,2-c]pyran] analogues with
RT bactericidal efficacy against Mycobacterium tuberculosis targeting MmpL3.";
RL PLoS ONE 8:E60933-E60933(2013).
RN [10]
RP ACTIVITY REGULATION, AND MECHANISM OF INHIBITION.
RX PubMed=25136022; DOI=10.1128/aac.03229-14;
RA Li W., Upadhyay A., Fontes F.L., North E.J., Wang Y., Crans D.C.,
RA Grzegorzewicz A.E., Jones V., Franzblau S.G., Lee R.E., Crick D.C.,
RA Jackson M.;
RT "Novel insights into the mechanism of inhibition of MmpL3, a target of
RT multiple pharmacophores in Mycobacterium tuberculosis.";
RL Antimicrob. Agents Chemother. 58:6413-6423(2014).
RN [11]
RP REVIEW.
RX PubMed=24325728; DOI=10.1517/14728222.2014.859677;
RA Rayasam G.V.;
RT "MmpL3 a potential new target for development of novel anti-tuberculosis
RT drugs.";
RL Expert Opin. Ther. Targets 18:247-256(2014).
CC -!- FUNCTION: Transports trehalose monomycolate (TMM) to the cell wall.
CC Flips TMM across the inner membrane (PubMed:22252828, PubMed:22344175).
CC Membrane potential is not required for this function. Transports
CC probably phosphatidylethanolamine (PE) as well. Binds specifically both
CC TMM and PE, but not trehalose dimycolate (TDM). Binds also
CC diacylglycerol (DAG) and other phospholipids, including
CC phosphatidylglycerol (PG), phosphatidylinositol (PI), and cardiolipin
CC (CDL). Contributes to membrane potential, cell wall composition,
CC antibiotic susceptibility and fitness (By similarity). Could also be
CC part of a heme-iron acquisition system (PubMed:21383189).
CC {ECO:0000250|UniProtKB:A0QP27, ECO:0000269|PubMed:22252828,
CC ECO:0000269|PubMed:22344175, ECO:0000305|PubMed:21383189}.
CC -!- FUNCTION: Is the target of the antitubercular drug SQ109.
CC {ECO:0000269|PubMed:22252828}.
CC -!- ACTIVITY REGULATION: Inhibited by the antitubercular drug SQ109. Also
CC inhibited by several other compounds such as the pyrrole derivative
CC BM212, the adamantyl urea derivative AU1235, the benzimidazole C215,
CC indoleamides, tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide (THPP)
CC and N-benzyl-6',7'-dihydrospiro[piperidine-4,4'-thieno[3,2-c]pyran]
CC (Spiro) analogs. Inhibitory effects of these compounds, including
CC SQ109, are most likely due to their ability to dissipate the
CC transmembrane electrochemical proton gradient.
CC {ECO:0000269|PubMed:22024828, ECO:0000269|PubMed:22252828,
CC ECO:0000269|PubMed:22344175, ECO:0000269|PubMed:22577943,
CC ECO:0000269|PubMed:23613759, ECO:0000269|PubMed:24352433,
CC ECO:0000269|PubMed:25136022}.
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 {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}. Cell septum
CC {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; AL123456; CCP42934.1; -; Genomic_DNA.
DR PIR; C70839; C70839.
DR RefSeq; NP_214720.1; NC_000962.3.
DR RefSeq; WP_003899855.1; NZ_NVQJ01000001.1.
DR PDB; 7NVH; EM; 3.02 A; A=1-753.
DR PDBsum; 7NVH; -.
DR AlphaFoldDB; P9WJV5; -.
DR SMR; P9WJV5; -.
DR STRING; 83332.Rv0206c; -.
DR PaxDb; P9WJV5; -.
DR DNASU; 886752; -.
DR GeneID; 886752; -.
DR KEGG; mtu:Rv0206c; -.
DR TubercuList; Rv0206c; -.
DR eggNOG; COG2409; Bacteria.
DR OMA; SRAYLNW; -.
DR PhylomeDB; P9WJV5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0030428; C:cell septum; ISS:UniProtKB.
DR GO; GO:0051286; C:cell tip; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
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:0071766; P:Actinobacterium-type cell wall biogenesis; IDA:MTBBASE.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0015920; P:lipopolysaccharide transport; IDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Cell wall biogenesis/degradation; Lipid transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..944
FT /note="Trehalose monomycolate exporter MmpL3"
FT /id="PRO_0000103564"
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"
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"
FT MUTAGEN 40
FT /note="Q->R: Confers resistance to SQ109."
FT /evidence="ECO:0000269|PubMed:22252828"
FT MUTAGEN 51
FT /note="V->A: Confers resistance to C215."
FT /evidence="ECO:0000269|PubMed:22577943"
FT MUTAGEN 215
FT /note="L->S: Confers resistance to BM212."
FT /evidence="ECO:0000269|PubMed:22024828"
FT MUTAGEN 253
FT /note="G->E: Increases resistance to AU1235."
FT /evidence="ECO:0000269|PubMed:22344175"
FT MUTAGEN 288
FT /note="S->T: Confers resistance to indoleamides."
FT /evidence="ECO:0000269|PubMed:24352433"
FT MUTAGEN 320
FT /note="L->P: Confers resistance to C215."
FT /evidence="ECO:0000269|PubMed:22577943"
FT MUTAGEN 567
FT /note="L->P: Confers resistance to SQ109."
FT /evidence="ECO:0000269|PubMed:22252828"
FT MUTAGEN 667
FT /note="T->A: Confers resistance to C215."
FT /evidence="ECO:0000269|PubMed:22577943"
FT MUTAGEN 684
FT /note="V->A: Confers resistance to C215."
FT /evidence="ECO:0000269|PubMed:22577943"
FT MUTAGEN 700
FT /note="A->T: Confers resistance to SQ109."
FT /evidence="ECO:0000269|PubMed:22252828"
FT HELIX 2..11
FT /evidence="ECO:0007829|PDB:7NVH"
FT TURN 15..21
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:7NVH"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:7NVH"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:7NVH"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 49..61
FT /evidence="ECO:0007829|PDB:7NVH"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:7NVH"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:7NVH"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:7NVH"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:7NVH"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:7NVH"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:7NVH"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:7NVH"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 176..200
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 203..227
FT /evidence="ECO:0007829|PDB:7NVH"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 248..265
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 270..297
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 305..336
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 337..340
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 385..391
FT /evidence="ECO:0007829|PDB:7NVH"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:7NVH"
FT TURN 396..400
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 401..408
FT /evidence="ECO:0007829|PDB:7NVH"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 434..443
FT /evidence="ECO:0007829|PDB:7NVH"
FT STRAND 451..458
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 466..476
FT /evidence="ECO:0007829|PDB:7NVH"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:7NVH"
FT STRAND 492..495
FT /evidence="ECO:0007829|PDB:7NVH"
FT STRAND 508..517
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 518..520
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 521..528
FT /evidence="ECO:0007829|PDB:7NVH"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:7NVH"
FT STRAND 540..543
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 544..556
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 559..577
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 582..606
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 612..615
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 624..654
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 659..669
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 671..689
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 694..712
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 714..726
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 728..731
FT /evidence="ECO:0007829|PDB:7NVH"
FT HELIX 735..743
FT /evidence="ECO:0007829|PDB:7NVH"
SQ 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
