SP2M_BACSU
ID SP2M_BACSU Reviewed; 214 AA.
AC P37873;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Stage II sporulation protein M;
GN Name=spoIIM; OrderedLocusNames=BSU23530;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; 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 / PY79;
RX PubMed=8501064; DOI=10.1128/jb.175.11.3607-3617.1993;
RA Smith K., Bayer M.E., Youngman P.;
RT "Physical and functional characterization of the Bacillus subtilis spoIIM
RT gene.";
RL J. Bacteriol. 175:3607-3617(1993).
RN [2]
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 [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).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / PY79;
RX PubMed=12502745; DOI=10.1101/gad.1039902;
RA Abanes-De Mello A., Sun Y.L., Aung S., Pogliano K.;
RT "A cytoskeleton-like role for the bacterial cell wall during engulfment of
RT the Bacillus subtilis forespore.";
RL Genes Dev. 16:3253-3264(2002).
RN [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF GLN-75; SER-76; ILE-92 AND LYS-107.
RC STRAIN=168 / PY79;
RX PubMed=17376078; DOI=10.1111/j.1365-2958.2007.05652.x;
RA Chastanet A., Losick R.;
RT "Engulfment during sporulation in Bacillus subtilis is governed by a multi-
RT protein complex containing tandemly acting autolysins.";
RL Mol. Microbiol. 64:139-152(2007).
CC -!- FUNCTION: Required for complete septum migration and engulfment of the
CC forespore compartment during sporulation. Required for stabilizing and
CC recruiting of SpoIIP to the septal membrane.
CC {ECO:0000269|PubMed:17376078, ECO:0000269|PubMed:8501064}.
CC -!- SUBUNIT: Component of the MPD complex composed of SpoIIM, SpoIIP and
CC SpoIID. {ECO:0000269|PubMed:17376078}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Note=Localizes to the sporulation septum and to
CC the second division site within the mother cell. Before the start of
CC engulfment localizes to the septal midpoint, then spreads throughout
CC the septum prior to becoming enriched at the leading edge of the
CC engulfing membrane, where it remains until the completion of membrane
CC migration. Some remain partially trapped at the septum during
CC engulfment and upon completion of engulfment become dispersed in the
CC outer forespore membrane. Localization of the MPD complex to the septal
CC membrane is dependent on SpoIIB. {ECO:0000269|PubMed:12502745,
CC ECO:0000269|PubMed:17376078}.
CC -!- DEVELOPMENTAL STAGE: Expression starts 2 hours post-sporulation.
CC {ECO:0000269|PubMed:8501064}.
CC -!- DISRUPTION PHENOTYPE: Results in a block at stage II of sporulation. No
CC fully engulfed forespores. SpoIIP mislocalization from the septal
CC membrane. {ECO:0000269|PubMed:17376078, ECO:0000269|PubMed:8501064}.
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DR EMBL; L06664; AAA75553.1; -; Genomic_DNA.
DR EMBL; D84432; BAA12647.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14285.1; -; Genomic_DNA.
DR PIR; A47581; A47581.
DR RefSeq; NP_390234.1; NC_000964.3.
DR RefSeq; WP_004398593.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P37873; -.
DR STRING; 224308.BSU23530; -.
DR TCDB; 9.B.98.2.1; the duf95 (duf95) family.
DR PaxDb; P37873; -.
DR PRIDE; P37873; -.
DR EnsemblBacteria; CAB14285; CAB14285; BSU_23530.
DR GeneID; 938723; -.
DR KEGG; bsu:BSU23530; -.
DR PATRIC; fig|224308.179.peg.2565; -.
DR eggNOG; COG1300; Bacteria.
DR OMA; QDLYYYL; -.
DR BioCyc; BSUB:BSU23530-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0030428; C:cell septum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1901893; P:positive regulation of cell septum assembly; IMP:UniProtKB.
DR GO; GO:0042173; P:regulation of sporulation resulting in formation of a cellular spore; IDA:UniProtKB.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR014196; SpoIIM.
DR InterPro; IPR002798; SpoIIM-like.
DR Pfam; PF01944; SpoIIM; 1.
DR PIRSF; PIRSF038973; SpoIIM; 1.
DR TIGRFAMs; TIGR02831; spo_II_M; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Sporulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..214
FT /note="Stage II sporulation protein M"
FT /id="PRO_0000072059"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..85
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..139
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..214
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT MUTAGEN 75
FT /note="Q->R: Partially restores the sporulation efficiency
FT of SpoIIP G-108 mutant."
FT /evidence="ECO:0000269|PubMed:17376078"
FT MUTAGEN 76
FT /note="S->R: Partially restores the sporulation efficiency
FT of SpoIIP G-108 mutant."
FT /evidence="ECO:0000269|PubMed:17376078"
FT MUTAGEN 92
FT /note="I->L: Has little or no effect on sporulation in
FT wild-type SpoIIP cells. Restores sporulation efficiency of
FT SpoIIP G-108 mutant almost to the level of the wild-type.
FT Localization of SpoIIP G-108 mutant to the septum is about
FT 78% that of wild-type SpoIIP. Fails to suppress the
FT sporulation defect of mutants SpoIIP R-189 and R-278 as
FT well as SpoIIP double mutant L-54 and P-114."
FT /evidence="ECO:0000269|PubMed:17376078"
FT MUTAGEN 107
FT /note="K->R: Partially restores the sporulation efficiency
FT of SpoIIP G-108 mutant."
FT /evidence="ECO:0000269|PubMed:17376078"
SQ SEQUENCE 214 AA; 24296 MW; F639C64F14A72E33 CRC64;
MRKISYKDMF LRHVKDHLSL YIFVSVLFFM GVIFGAIIVN SMTISQKEDL YYYLSQFFGQ
LSDGKQASSA DMFGQSIFHN AKYLGLMWIL GISVIGMPII FIMIFLKGIV VGFTVGFLVN
QMGVSGFFLS FVSVLPQNVL LIPAYLIMGT CAIAFSLKLI RQLFVKRSLH DAPIQWFGRY
AFVLLVILFL ALISSLFEAY LSPVLMEKLT SRLF
