MSTX_BACSU
ID MSTX_BACSU Reviewed; 110 AA.
AC Q5BU39; O05247;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Protein mistic;
DE AltName: Full=Membrane-integrating protein MstX;
GN Name=mstX; OrderedLocusNames=BSU31321; ORFNames=BSU31320;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9274030; DOI=10.1099/00221287-143-8-2769;
RA Oudega B., Koningstein G., Rodrigues L., de Sales Ramon M., Hilbert H.,
RA Duesterhoeft A., Pohl T.M., Weitzenegger T.;
RT "Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence
RT of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai).";
RL Microbiology 143:2769-2774(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], STRUCTURE BY NMR, TOPOLOGY, FUNCTION AS
RP A CHAPERONE, SUBUNIT, SUBCELLULAR LOCATION, BIOTECHNOLOGY, AND MUTAGENESIS
RP OF TRP-13 AND MET-75.
RX PubMed=15731457; DOI=10.1126/science.1106392;
RA Roosild T.P., Greenwald J., Vega M., Castronovo S., Riek R., Choe S.;
RT "NMR structure of Mistic, a membrane-integrating protein for membrane
RT protein expression.";
RL Science 307:1317-1321(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Chaperone that facilitates the production and integration of
CC integral membrane proteins into the bacterial lipid bilayer.
CC {ECO:0000269|PubMed:15731457}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15731457}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15731457};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15731457}. Note=Folds
CC autonomously into the membrane, bypassing the cellular translocon
CC machinery.
CC -!- BIOTECHNOLOGY: As a fusion partner, can be used for high-level
CC production of other membrane proteins in their native conformations,
CC including many eukaryotic proteins that have previously been
CC intractable to bacterial expression. {ECO:0000269|PubMed:15731457}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB07933.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z93936; CAB07933.1; ALT_TERM; Genomic_DNA.
DR EMBL; AY874162; AAX20121.1; -; Genomic_DNA.
DR EMBL; AL009126; CAX52684.1; -; Genomic_DNA.
DR RefSeq; WP_003228886.1; NZ_JNCM01000033.1.
DR RefSeq; YP_003097778.1; NC_000964.3.
DR PDB; 1YGM; NMR; -; A=1-110.
DR PDBsum; 1YGM; -.
DR AlphaFoldDB; Q5BU39; -.
DR SMR; Q5BU39; -.
DR STRING; 224308.BSU31321; -.
DR TCDB; 9.A.66.1.1; the mistic (mistic) family.
DR PRIDE; Q5BU39; -.
DR EnsemblBacteria; CAX52684; CAX52684; BSU_31321.
DR GeneID; 8303011; -.
DR KEGG; bsu:BSU31321; -.
DR PATRIC; fig|224308.179.peg.3395; -.
DR eggNOG; ENOG50338PF; Bacteria.
DR OMA; FCSFFEK; -.
DR BioCyc; BSUB:BSU31321-MON; -.
DR EvolutionaryTrace; Q5BU39; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 1.10.220.90; -; 1.
DR InterPro; IPR021078; Membrane-integrating_Mistic.
DR InterPro; IPR038193; Mistic_sf.
DR Pfam; PF11458; Mistic; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Chaperone; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..110
FT /note="Protein mistic"
FT /id="PRO_0000390881"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15731457"
FT TRANSMEM 8..22
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 23..31
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:15731457"
FT TRANSMEM 32..55
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 56..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15731457"
FT TRANSMEM 67..81
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 82..88
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:15731457"
FT TRANSMEM 89..102
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 103..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15731457"
FT MUTAGEN 13
FT /note="W->A: Decrease in functionality."
FT /evidence="ECO:0000269|PubMed:15731457"
FT MUTAGEN 75
FT /note="M->A: Destabilization of structural stability and
FT loss of functionality."
FT /evidence="ECO:0000269|PubMed:15731457"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:1YGM"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:1YGM"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:1YGM"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:1YGM"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:1YGM"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:1YGM"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:1YGM"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1YGM"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:1YGM"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:1YGM"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:1YGM"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:1YGM"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:1YGM"
SQ SEQUENCE 110 AA; 12833 MW; AC8FDF2B33B9152A CRC64;
MFCTFFEKHH RKWDILLEKS TGVMEAMKVT SEEKEQLSTA IDRMNEGLDA FIQLYNESEI
DEPLIQLDDD TAELMKQARD MYGQEKLNEK LNTIIKQILS ISVSEEGEKE
