MISCB_BACSU
ID MISCB_BACSU Reviewed; 275 AA.
AC P54544;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Membrane protein insertase MisCB;
DE AltName: Full=Foldase YidC 1;
DE AltName: Full=Membrane integrase YidC 1;
DE AltName: Full=Membrane protein YidC 1;
DE Flags: Precursor;
GN Name=misCB; Synonyms=yqjG; OrderedLocusNames=BSU23890;
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 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP INTERACTION WITH SPOIIIAE, AND SUBUNIT.
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 [7]
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 [8]
RP FUNCTION IN GENETIC COMPETENCE DEVELOPMENT, AND 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. It has an overlapping, although partly distinct,
CC function compared to SpoIIIJ(MisCB). {ECO:0000250,
CC ECO:0000269|PubMed:11889108, ECO:0000269|PubMed:12586834,
CC ECO:0000269|PubMed:21204254}.
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: Predominantly expressed in vegetative cells.
CC {ECO:0000269|PubMed:11889108, ECO:0000269|PubMed:12586834}.
CC -!- DISRUPTION PHENOTYPE: Disruption decreases genetic competence by about
CC 50%, significant loss of expression of ComGC, no effect on sporulation.
CC A double spoIIIJ-yqjG deletion is lethal. {ECO:0000269|PubMed:11889108,
CC ECO:0000269|PubMed:12586834, ECO:0000269|PubMed:21204254}.
CC -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 2 subfamily.
CC {ECO:0000305}.
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DR EMBL; D84432; BAA12613.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14320.1; -; Genomic_DNA.
DR PIR; G69963; G69963.
DR RefSeq; NP_390269.1; NC_000964.3.
DR RefSeq; WP_003230359.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P54544; -.
DR SMR; P54544; -.
DR IntAct; P54544; 10.
DR STRING; 224308.BSU23890; -.
DR TCDB; 2.A.9.3.3; the membrane protein insertase (yidc/alb3/oxa1) family.
DR PaxDb; P54544; -.
DR PRIDE; P54544; -.
DR DNASU; 938692; -.
DR EnsemblBacteria; CAB14320; CAB14320; BSU_23890.
DR GeneID; 938692; -.
DR KEGG; bsu:BSU23890; -.
DR PATRIC; fig|224308.179.peg.2602; -.
DR eggNOG; COG0706; Bacteria.
DR InParanoid; P54544; -.
DR OMA; IYWIASS; -.
DR PhylomeDB; P54544; -.
DR BioCyc; BSUB:BSU23890-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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 HAMAP; MF_01811; YidC_type2; 1.
DR InterPro; IPR028055; Membr_insert_YidC/Oxa1_C.
DR InterPro; IPR001708; YidC/ALB3/OXA1/COX18.
DR InterPro; IPR023060; YidC/YidC1/YidC2_Firmicutes.
DR PANTHER; PTHR12428; PTHR12428; 1.
DR Pfam; PF02096; 60KD_IMP; 1.
DR TIGRFAMs; TIGR03592; yidC_oxa1_cterm; 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..275
FT /note="Membrane protein insertase MisCB"
FT /id="PRO_0000020379"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 275 AA; 30748 MW; 9BAD79A2BABEA53B CRC64;
MLKTYQKLLA MGIFLIVLCS GNAAFAATNQ VGGLSNVGFF HDYLIEPFSA LLKGVAGLFH
GEYGLSIILV TIIVRIVVLP LFVNQFKKQR IFQEKMAVIK PQVDSIQVKL KKTKDPEKQK
ELQMEMMKLY QEHNINPLAM GCLPMLIQSP IMIGLYYAIR STPEIASHSF LWFSLGQSDI
LMSLSAGIMY FVQAYIAQKL SAKYSAVPQN PAAQQSAKLM VFIFPVMMTI FSLNVPAALP
LYWFTSGLFL TVQNIVLQMT HHKSKKTAAL TESVK
