MMPLB_MYCTU
ID MMPLB_MYCTU Reviewed; 966 AA.
AC P9WJT9; L0T2Z6; O53653; P65374;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Heme uptake protein MmpL11 {ECO:0000305};
GN Name=mmpL11; OrderedLocusNames=Rv0202c; ORFNames=MTV033.10c;
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 FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=15908378; DOI=10.1128/iai.73.6.3492-3501.2005;
RA Domenech P., Reed M.B., Barry C.E. III;
RT "Contribution of the Mycobacterium tuberculosis MmpL protein family to
RT virulence and drug resistance.";
RL Infect. Immun. 73:3492-3501(2005).
RN [3]
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 [4]
RP PROBABLE FUNCTION IN HEME UPTAKE, 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 [5]
RP FUNCTION IN HEME UPTAKE, AND HEME BINDING.
RX PubMed=23760277; DOI=10.1074/jbc.m113.453076;
RA Owens C.P., Chim N., Graves A.B., Harmston C.A., Iniguez A., Contreras H.,
RA Liptak M.D., Goulding C.W.;
RT "The Mycobacterium tuberculosis secreted protein Rv0203 transfers heme to
RT membrane proteins MmpL3 and MmpL11.";
RL J. Biol. Chem. 288:21714-21728(2013).
RN [6]
RP PUTATIVE FUNCTION IN MYCOLIC ACID-CONTAINING LIPIDS EXPORT.
RC STRAIN=H37Rv;
RX PubMed=23836904; DOI=10.1074/jbc.m113.473371;
RA Pacheco S.A., Hsu F.F., Powers K.M., Purdy G.E.;
RT "MmpL11 protein transports mycolic acid-containing lipids to the
RT mycobacterial cell wall and contributes to biofilm formation in
RT Mycobacterium smegmatis.";
RL J. Biol. Chem. 288:24213-24222(2013).
CC -!- FUNCTION: Part of a heme-iron acquisition system. Receives heme from
CC the heme-binding protein Rv0203 and transports it into the
CC mycobacterial cell. Contributes to virulence.
CC {ECO:0000269|PubMed:15908378, ECO:0000269|PubMed:21383189,
CC ECO:0000269|PubMed:23760277}.
CC -!- FUNCTION: Could also transport the mycolic acid-containing lipids
CC monomeromycolyl diacylglycerol (MMDAG) and mycolate ester wax (WE) to
CC the bacterial surface. {ECO:0000303|PubMed:23836904}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:23760277}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Inactivation increases mouse survival. Mutants
CC show growth patterns similar to the wild-type strain during the active
CC growth phase, but they are attenuated for survival in the chronic
CC stages of infection. {ECO:0000269|PubMed:15908378}.
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; CCP42930.1; -; Genomic_DNA.
DR PIR; G70838; G70838.
DR RefSeq; NP_214716.1; NC_000962.3.
DR RefSeq; WP_003401190.1; NZ_NVQJ01000001.1.
DR PDB; 4Y0L; X-ray; 2.40 A; A=424-511.
DR PDBsum; 4Y0L; -.
DR AlphaFoldDB; P9WJT9; -.
DR SMR; P9WJT9; -.
DR STRING; 83332.Rv0202c; -.
DR PaxDb; P9WJT9; -.
DR DNASU; 886750; -.
DR GeneID; 886750; -.
DR KEGG; mtu:Rv0202c; -.
DR TubercuList; Rv0202c; -.
DR eggNOG; COG2409; Bacteria.
DR OMA; HWSRRPE; -.
DR PhylomeDB; P9WJT9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Virulence.
FT CHAIN 1..966
FT /note="Heme uptake protein MmpL11"
FT /id="PRO_0000103577"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 595..615
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 668..688
FT /note="Helical"
FT /evidence="ECO:0000255"
FT STRAND 425..430
FT /evidence="ECO:0007829|PDB:4Y0L"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:4Y0L"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:4Y0L"
FT HELIX 442..452
FT /evidence="ECO:0007829|PDB:4Y0L"
FT STRAND 471..478
FT /evidence="ECO:0007829|PDB:4Y0L"
FT HELIX 489..503
FT /evidence="ECO:0007829|PDB:4Y0L"
FT STRAND 506..510
FT /evidence="ECO:0007829|PDB:4Y0L"
SQ SEQUENCE 966 AA; 103502 MW; 3E8BF0327CBEA2DA CRC64;
MMRLSRNLRR CRWLVFTGWL LALVPAVYLA MTQSGNLTGG GFEVAGSQSL LVHDQLDAHY
PDRGAPALAL VAAPRPDASY QDIDNAVALL RQIASELPGV TEAPNPTQRP PQPDRPYVVS
LRLDARNAGT SDVAKKLRDR IGVKGDQSGQ TANGKVRLYV IGQGALSAAA AANTKHDIAN
AERWNLPIIL MVLVAVFGSL AAAAIPLALA VCTVVITMGL VFVLSMHTTM SVFVTSTVSM
FGIALAVDYS LFILMRYREE LRCGRRPPDA VDAAMATSGL AVVLSGMTVI ASLTGIYLIN
TPALRSMATG AILAVAVAML TSATLTPAVL ATFARAAAKR SALVHWSRRP ASTQSWFWSR
WVGWVMRRPW ITALAASTVL LVMAAPATLM VLGNSLLRQF DSSHEIRTGA AAAAQALGPG
ALGPVQVLVR FDAGGASAPE HSQTIAAIRH RIAQAPNVVS VAPPRFADDN GSALLSAVLS
VDPEDLGARD TITWMRTQLP RVAGAAQVDV GGPTALIKDF DDRVSATQPL VLVFVAVIAF
LMLLISIRSV FLAFKGVLMT LLSVAAAYGS LVMVFQWGWA RGLGFPALHS IDSTVPPLVL
AMTFGLSMDY EIFLLTRIRE RFLQTGQTRD AVAYGVRTSA RTITSAALIM IAVFCGFAFA
GMPLVAEIGV ACAVAIAVDA TVVRLVLVPA LMAMFDRWNW WLPRWLAHIL PSVDFDRPLP
KVDLGDVVVI PDDFAAAIPP SADVRMVLKS AAKLKRLAPD AICVTDPLAF TGCGCDGKAL
DQVQLAYRNG IARAISWGQR PVHPVTVWRK RLAVALDALQ TTTWECGGVQ THRAGPGYRR
RSPVETTNVA LPTGDRLQIP TGAETLRFKG YLIMSRNSSH DYADFADLVD TMAPETAAAV
LAGMDRYYSC QAPGRQWMAT QLVGRLADPQ PSDLGDQSPG ADAQAKWEEV RRRCLSVAVA
MLEEAR
