ID MISCA_BACSU Reviewed; 261 AA.
AC Q01625; O32298;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 27-MAR-2024, entry version 150.
DE RecName: Full=Membrane protein insertase MisCA;
DE AltName: Full=Foldase YidC 2;
DE AltName: Full=Membrane integrase YidC 2;
DE AltName: Full=Membrane protein YidC 2;
DE AltName: Full=Stage III sporulation protein J;
DE Short=SpoIIIJ;
DE Flags: Precursor;
GN Name=misCA; Synonyms=spoIIIJ; OrderedLocusNames=BSU41040;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=1487728; DOI=10.1099/00221287-138-12-2609;
RA Errington J., Appleby L., Daniel R.A., Goodfellow H., Partridge S.R.,
RA Yudkin M.D.;
RT "Structure and function of the spoIIIJ gene of Bacillus subtilis: a
RT vegetatively expressed gene that is essential for sigma G activity at an
RT intermediate stage of sporulation.";
RL J. Gen. Microbiol. 138:2609-2618(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / CRK2000;
RX PubMed=1552862; DOI=10.1111/j.1365-2958.1992.tb01510.x;
RA Ogasawara N., Yoshikawa H.;
RT "Genes and their organization in the replication origin region of the
RT bacterial chromosome.";
RL Mol. Microbiol. 6:629-634(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [4]
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168;
RX PubMed=11889108; DOI=10.1128/jb.184.7.1998-2004.2002;
RA Murakami T., Haga K., Takeuchi M., Sato T.;
RT "Analysis of the Bacillus subtilis spoIIIJ gene and its paralogue gene,
RT yqjG.";
RL J. Bacteriol. 184:1998-2004(2002).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=12586834; DOI=10.1074/jbc.m301205200;
RA Tjalsma H., Bron S., van Dijl J.M.;
RT "Complementary impact of paralogous Oxa1-like proteins of Bacillus subtilis
RT on post-translocational stages in protein secretion.";
RL J. Biol. Chem. 278:15622-15632(2003).
RN [7]
RP FUNCTION IN SPORULATION.
RC STRAIN=168 / MB24;
RX PubMed=12813085; DOI=10.1128/jb.185.13.3905-3917.2003;
RA Serrano M., Corte L., Opdyke J., Moran C.P. Jr., Henriques A.O.;
RT "Expression of spoIIIJ in the prespore is sufficient for activation of
RT sigma G and for sporulation in Bacillus subtilis.";
RL J. Bacteriol. 185:3905-3917(2003).
RN [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / PY79;
RX PubMed=15995216; DOI=10.1128/jb.187.14.5000-5002.2005;
RA Rubio A., Jiang X., Pogliano K.;
RT "Localization of translocation complex components in Bacillus subtilis:
RT enrichment of the signal recognition particle receptor at early sporulation
RT septa.";
RL J. Bacteriol. 187:5000-5002(2005).
RN [9]
RP INTERACTION WITH SPOIIIAE, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / MB24;
RX PubMed=18820020; DOI=10.1128/jb.00715-08;
RA Serrano M., Vieira F., Moran C.P. Jr., Henriques A.O.;
RT "Processing of a membrane protein required for cell-to-cell signaling
RT during endospore formation in Bacillus subtilis.";
RL J. Bacteriol. 190:7786-7796(2008).
RN [10]
RP INTERACTION WITH F(1)F(0) ATP SYNTHASE COMPLEX AND YQGA, AND COMPLEMENTS
RP E.COLI.
RC STRAIN=168;
RX PubMed=19717609; DOI=10.1128/jb.00853-09;
RA Saller M.J., Fusetti F., Driessen A.J.;
RT "Bacillus subtilis SpoIIIJ and YqjG function in membrane protein
RT biogenesis.";
RL J. Bacteriol. 191:6749-6757(2009).
RN [11]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=21204254; DOI=10.1002/pmic.201000435;
RA Saller M.J., Otto A., Berrelkamp-Lahpor G.A., Becher D., Hecker M.,
RA Driessen A.J.;
RT "Bacillus subtilis YqjG is required for genetic competence development.";
RL Proteomics 11:270-282(2011).
CC -!- FUNCTION: Required for the insertion and/or proper folding and/or
CC complex formation of integral membrane proteins into the membrane.
CC Involved in integration of membrane proteins that insert both
CC dependently and independently of the Sec translocase complex, as well
CC as at least some lipoproteins (By similarity). Also involved in protein
CC secretion processes. Essential for sporulation by activating sigma
CC factor SpoIIIG/SigG after engulfment is completed in the prespore,
CC maybe by acting on SpoIIIAE. It has an overlapping, although partly
CC distinct, function compared to YqjG(MisCB). {ECO:0000250,
CC ECO:0000269|PubMed:11889108, ECO:0000269|PubMed:12586834,
CC ECO:0000269|PubMed:12813085, ECO:0000269|PubMed:1487728}.
CC -!- SUBUNIT: Mostly monomeric, it may also form dimers. Interacts with
CC SpoIIIAE. Forms a complex with the F(1)F(0) ATP synthase in which can
CC be found the alpha, beta, gamma, delta and epsilon subunits of F(1) and
CC a, b and subunits of F(0). YqgA is found in the same complex.
CC {ECO:0000269|PubMed:18820020, ECO:0000269|PubMed:19717609}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11889108,
CC ECO:0000269|PubMed:15995216}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11889108, ECO:0000269|PubMed:15995216}. Note=Found
CC uniformly distributed in both the mother cell and forespore following
CC sporulation.
CC -!- DEVELOPMENTAL STAGE: SpoIIIJ is required only after engulfment and
CC turned off at the onset of sporulation. While it is predominantly
CC expressed in vegetative cells, its low expression after the onset of
CC sporulation is essential for sporulation to occur.
CC {ECO:0000269|PubMed:11889108, ECO:0000269|PubMed:12586834,
CC ECO:0000269|PubMed:1487728}.
CC -!- DISRUPTION PHENOTYPE: Essential for sporulation, disruption affects the
CC expression of prespore-specific genes but not early mother-cell-
CC specific genes, i.e. cells do not progress beyond stage III of
CC sporulation. A double spoIIIJ-yqjG deletion is lethal. Genetic
CC competence increases about 20-fold in the single disruption.
CC {ECO:0000269|PubMed:11889108, ECO:0000269|PubMed:12586834,
CC ECO:0000269|PubMed:1487728, ECO:0000269|PubMed:18820020,
CC ECO:0000269|PubMed:21204254}.
CC -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 2 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA78595.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z14225; CAA78595.1; ALT_INIT; Genomic_DNA.
DR EMBL; X62539; CAA44401.1; -; Genomic_DNA.
DR EMBL; D26185; BAA05234.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16141.1; -; Genomic_DNA.
DR PIR; I40437; I40437.
DR RefSeq; NP_391984.1; NC_000964.3.
DR RefSeq; WP_010886648.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; Q01625; -.
DR SMR; Q01625; -.
DR IntAct; Q01625; 10.
DR STRING; 224308.BSU41040; -.
DR TCDB; 2.A.9.3.2; the membrane protein insertase (yidc/alb3/oxa1) family.
DR PaxDb; 224308-BSU41040; -.
DR DNASU; 937934; -.
DR EnsemblBacteria; CAB16141; CAB16141; BSU_41040.
DR GeneID; 937934; -.
DR KEGG; bsu:BSU41040; -.
DR PATRIC; fig|224308.43.peg.4313; -.
DR eggNOG; COG0706; Bacteria.
DR InParanoid; Q01625; -.
DR OrthoDB; 9780552at2; -.
DR PhylomeDB; Q01625; -.
DR BioCyc; BSUB:BSU41040-MONOMER; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032977; F:membrane insertase activity; IBA:GO_Central.
DR GO; GO:0051205; P:protein insertion into membrane; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd20070; 5TM_YidC_Alb3; 1.
DR HAMAP; MF_01811; YidC_type2; 1.
DR InterPro; IPR001708; YidC/ALB3/OXA1/COX18.
DR InterPro; IPR028055; YidC/Oxa/ALB_C.
DR InterPro; IPR023060; YidC/YidC1/YidC2_Firmicutes.
DR InterPro; IPR047196; YidC_ALB_C.
DR NCBIfam; TIGR03592; yidC_oxa1_cterm; 1.
DR PANTHER; PTHR12428:SF65; INNER MEMBRANE PROTEIN ALBINO3, CHLOROPLASTIC; 1.
DR PANTHER; PTHR12428; OXA1; 1.
DR Pfam; PF02096; 60KD_IMP; 1.
DR PRINTS; PR00701; 60KDINNERMP.
DR PRINTS; PR01900; YIDCPROTEIN.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Chaperone; Lipoprotein; Membrane; Palmitate;
KW Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..261
FT /note="Membrane protein insertase MisCA"
FT /id="PRO_0000020378"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT LIPID 23
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 23
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 261 AA; 29522 MW; F211200B8CEBBEC5 CRC64;
MLLKRRIGLL LSMVGVFMLL AGCSSVKEPI TADSPHFWDK YVVYPLSELI TYVAKLTGDN
YGLSIILVTI LIRLLILPLM IKQLRSSKAM QALQPEMQKL KEKYSSKDQK TQQKLQQETM
ALFQKHGVNP LAGCFPILIQ MPILIGFYHA IMRTQAISEH SFLWFDLGEK DPYYILPIVA
GVATFVQQKL MMAGNAQQNP QMAMMLWIMP IMIIVFAINF PAALSLYWVV GNLFMIAQTF
LIKGPDIKKN PEPQKAGGKK K
//
