MIFM_BACSU
ID MIFM_BACSU Reviewed; 95 AA.
AC Q7WY64;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Membrane protein insertion and folding monitor;
DE AltName: Full=Sensor of SpoIIIJ activity;
GN Name=mifM; Synonyms=yqzJ; OrderedLocusNames=BSU23880;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, GENE NAME, AND MUTAGENESIS OF ILE-65;
RP TYR-67; HIS-68; ARG-69; ILE-70; THR-71; TRP-73; ILE-74; MET-80; ASN-81;
RP GLU-88 AND ASP-89.
RC STRAIN=168 / PY79;
RX PubMed=19779460; DOI=10.1038/emboj.2009.280;
RA Chiba S., Lamsa A., Pogliano K.;
RT "A ribosome-nascent chain sensor of membrane protein biogenesis in Bacillus
RT subtilis.";
RL EMBO J. 28:3461-3475(2009).
RN [3]
RP FUNCTION.
RX PubMed=21383133; DOI=10.1073/pnas.1018343108;
RA Chiba S., Kanamori T., Ueda T., Akiyama Y., Pogliano K., Ito K.;
RT "Recruitment of a species-specific translational arrest module to monitor
RT different cellular processes.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:6073-6078(2011).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF 86-ASP--ASP-89.
RC STRAIN=168 / PY79;
RX PubMed=22864117; DOI=10.1016/j.molcel.2012.06.034;
RA Chiba S., Ito K.;
RT "Multisite ribosomal stalling: a unique mode of regulatory nascent chain
RT action revealed for MifM.";
RL Mol. Cell 47:863-872(2012).
CC -!- FUNCTION: Sensor protein that up-regulates translation of the secondary
CC membrane protein insertase (MisCB/YqjG) when activity of the primary
CC membrane protein insertase (MisCA/SpoIIIJ) is limited. Acts as a
CC ribosome-nascent chain complex. When the primary membrane protein
CC insertase activity or level is reduced, the membrane insertion of MifM
CC is impaired, which induces arrest of MifM translation and unfolding of
CC the mRNA hairpin. Unfolding leads to translation of the downstream
CC gene, which encodes the secondary membrane protein insertase
CC MisCB/YqjG. Translation arrest of MifM is mediated by interaction of
CC its C-terminal domain with the ribosomal polypeptide exit tunnel.
CC Undergoes multisite stalling, which may allow a sufficient duration of
CC ribosomal stalling and consequently sufficient levels of MisCB/YqjG.
CC {ECO:0000269|PubMed:19779460, ECO:0000269|PubMed:21383133,
CC ECO:0000269|PubMed:22864117}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19779460};
CC Single-pass membrane protein {ECO:0000269|PubMed:19779460}.
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DR EMBL; AL009126; CAE01460.1; -; Genomic_DNA.
DR RefSeq; WP_010886563.1; NZ_JNCM01000036.1.
DR RefSeq; YP_054586.1; NC_000964.3.
DR PDB; 3J9W; EM; 3.90 A; AZ=1-95.
DR PDBsum; 3J9W; -.
DR AlphaFoldDB; Q7WY64; -.
DR SMR; Q7WY64; -.
DR STRING; 224308.BSU23880; -.
DR PaxDb; Q7WY64; -.
DR PRIDE; Q7WY64; -.
DR EnsemblBacteria; CAE01460; CAE01460; BSU_23880.
DR GeneID; 2914225; -.
DR KEGG; bsu:BSU23880; -.
DR PATRIC; fig|224308.43.peg.2491; -.
DR OMA; YHRITTW; -.
DR BioCyc; BSUB:BSU23880-MON; -.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..95
FT /note="Membrane protein insertion and folding monitor"
FT /id="PRO_0000049855"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 86..89
FT /note="Crucial for elongation arrest"
FT MUTAGEN 65
FT /note="I->A: Increases accumulation of full-length MifM."
FT /evidence="ECO:0000269|PubMed:19779460"
FT MUTAGEN 67
FT /note="Y->A: Reduces misCB/yqjG induction in misCA/spoIIIJ
FT mutant."
FT /evidence="ECO:0000269|PubMed:19779460"
FT MUTAGEN 68
FT /note="H->A: Increases accumulation of full-length MifM."
FT /evidence="ECO:0000269|PubMed:19779460"
FT MUTAGEN 69
FT /note="R->A: Increases accumulation of full-length MifM.
FT Reduces misCB/yqjG induction in misCA/spoIIIJ mutant."
FT /evidence="ECO:0000269|PubMed:19779460"
FT MUTAGEN 70
FT /note="I->A: Increases accumulation of full-length MifM.
FT Reduces misCB/yqjG induction in misCA/spoIIIJ mutant."
FT /evidence="ECO:0000269|PubMed:19779460"
FT MUTAGEN 71
FT /note="T->A: Reduces misCB/yqjG induction in misCA/spoIIIJ
FT mutant."
FT /evidence="ECO:0000269|PubMed:19779460"
FT MUTAGEN 73
FT /note="W->A: Increases accumulation of full-length MifM.
FT Reduces misCB/yqjG induction in misCA/spoIIIJ mutant."
FT /evidence="ECO:0000269|PubMed:19779460"
FT MUTAGEN 74
FT /note="I->A: Increases accumulation of full-length MifM.
FT Reduces misCB/yqjG induction in misCA/spoIIIJ mutant."
FT /evidence="ECO:0000269|PubMed:19779460"
FT MUTAGEN 80
FT /note="M->A: Increases accumulation of full-length MifM.
FT Reduces misCB/yqjG induction in misCA/spoIIIJ mutant."
FT /evidence="ECO:0000269|PubMed:19779460"
FT MUTAGEN 81
FT /note="N->A: Increases accumulation of full-length MifM.
FT Reduces misCB/yqjG induction in misCA/spoIIIJ mutant."
FT /evidence="ECO:0000269|PubMed:19779460"
FT MUTAGEN 86..89
FT /note="DEED->AAAA,KKKK: Lack of activity."
FT /evidence="ECO:0000269|PubMed:22864117"
FT MUTAGEN 86..89
FT /note="DEED->EDDE,EEEE: No change in activity."
FT /evidence="ECO:0000269|PubMed:22864117"
FT MUTAGEN 87..88
FT /note="EE->DD: No change in activity."
FT MUTAGEN 88
FT /note="E->A: Minor effects on translational arrest."
FT /evidence="ECO:0000269|PubMed:19779460"
FT MUTAGEN 89
FT /note="D->A: Minor effects on translational arrest."
FT /evidence="ECO:0000269|PubMed:19779460"
SQ SEQUENCE 95 AA; 11144 MW; 7295E6C084540065 CRC64;
MTMFVESIND VLFLVDFFTI ILPALTAIGI AFLLRECRAG EQWKSKRTDE HQTVFHINRT
DFLIIIYHRI TTWIRKVFRM NSPVNDEEDA GSLLL
