(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 93.
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}.
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   STRING; 224308.BSU23530; -.
DR   TCDB; 9.B.98.2.1; the duf95 (duf95) family.
DR   PaxDb; P37873; -.
DR   PRIDE; P37873; -.
DR   EnsemblBacteria; CAB14285; CAB14285; BSU23530.
DR   GeneID; 938723; -.
DR   KEGG; bsu:BSU23530; -.
DR   PATRIC; fig|224308.179.peg.2565; -.
DR   eggNOG; ENOG4105MZ9; Bacteria.
DR   eggNOG; COG1300; LUCA.
DR   HOGENOM; HOG000057761; -.
DR   KO; K06384; -.
DR   OMA; QDLYYYL; -.
DR   BioCyc; BSUB:BSU23530-MONOMER; -.
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;
DR   PRODOM; P37873.
DR   SWISS-2DPAGE; P37873.
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
//

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