SPOVM_BACSU
ID SPOVM_BACSU Reviewed; 26 AA.
AC P37817;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Stage V sporulation protein M {ECO:0000305};
GN Name=spoVM {ECO:0000303|PubMed:8231808}; OrderedLocusNames=BSU15810;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=168 / PY79;
RX PubMed=8231808; DOI=10.1111/j.1365-2958.1993.tb01736.x;
RA Levin P.A., Fan N., Ricca E., Driks A., Losick R., Cutting S.M.;
RT "An unusually small gene required for sporulation by Bacillus subtilis.";
RL Mol. Microbiol. 9:761-771(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9534248; DOI=10.1099/00221287-144-3-801;
RA Foulger D., Errington J.;
RT "A 28 kbp segment from the spoVM region of the Bacillus subtilis 168
RT genome.";
RL Microbiology 144:801-805(1998).
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 FUNCTION, AND INTERACTION WITH FTSH.
RC STRAIN=168 / PY79;
RX PubMed=9287010; DOI=10.1128/jb.179.17.5534-5542.1997;
RA Cutting S., Anderson M., Lysenko E., Page A., Tomoyasu T., Tatematsu K.,
RA Tatsuta T., Kroos L., Ogura T.;
RT "SpoVM, a small protein essential to development in Bacillus subtilis,
RT interacts with the ATP-dependent protease FtsH.";
RL J. Bacteriol. 179:5534-5542(1997).
RN [5]
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF LYS-2; PHE-3; TYR-4;
RP ILE-6; LEU-8; PRO-9; LEU-12; ILE-15 AND ARG-17.
RC STRAIN=168 / PY79;
RX PubMed=12562810; DOI=10.1128/jb.185.4.1391-1398.2003;
RA van Ooij C., Losick R.;
RT "Subcellular localization of a small sporulation protein in Bacillus
RT subtilis.";
RL J. Bacteriol. 185:1391-1398(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SPOIVA.
RX PubMed=17427285; DOI=10.1111/j.1365-2958.2006.05468.x;
RA Ramamurthi K.S., Clapham K.R., Losick R.;
RT "Peptide anchoring spore coat assembly to the outer forespore membrane in
RT Bacillus subtilis.";
RL Mol. Microbiol. 62:1547-1557(2006).
RN [7]
RP INDUCTION.
RX PubMed=18820968; DOI=10.1007/s00284-008-9273-y;
RA Le A.T., Schumann W.;
RT "Regulation of the spoVM gene of Bacillus subtilis.";
RL Curr. Microbiol. 57:484-489(2008).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ILE-15.
RX PubMed=22463703; DOI=10.1111/j.1365-2958.2012.08052.x;
RA Ebmeier S.E., Tan I.S., Clapham K.R., Ramamurthi K.S.;
RT "Small proteins link coat and cortex assembly during sporulation in
RT Bacillus subtilis.";
RL Mol. Microbiol. 84:682-696(2012).
RN [9]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-9.
RX PubMed=29102609; DOI=10.1016/j.cels.2017.10.004;
RA Kim E.Y., Tyndall E.R., Huang K.C., Tian F., Ramamurthi K.S.;
RT "Dash-and-recruit mechanism drives membrane curvature recognition by the
RT small bacterial protein SpoVM.";
RL Cell Syst. 5:518-526(2017).
RN [10]
RP BIOTECHNOLOGY.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=22882210; DOI=10.1111/j.1365-2958.2012.08205.x;
RA Yepes A., Schneider J., Mielich B., Koch G., Garcia-Betancur J.C.,
RA Ramamurthi K.S., Vlamakis H., Lopez D.;
RT "The biofilm formation defect of a Bacillus subtilis flotillin-defective
RT mutant involves the protease FtsH.";
RL Mol. Microbiol. 86:457-471(2012).
RN [11] {ECO:0007744|PDB:2MVH, ECO:0007744|PDB:2MVJ}
RP STRUCTURE BY NMR, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-17.
RC STRAIN=168 / PY79;
RX PubMed=25825747; DOI=10.1073/pnas.1423868112;
RA Gill R.L. Jr., Castaing J.P., Hsin J., Tan I.S., Wang X., Huang K.C.,
RA Tian F., Ramamurthi K.S.;
RT "Structural basis for the geometry-driven localization of a small
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E1908-E1915(2015).
CC -!- FUNCTION: Coordinates cortex and coat assembly during sporulation
CC (PubMed:22463703, PubMed:8231808). Associates with the spore coat
CC protein SpoIVA and with the outer forespore membrane, thereby serving
CC as a membrane anchor that tethers SpoIVA and the entire spore coat to
CC the forespore surface (PubMed:17427285). May also serve as a
CC competitive inhibitor of FtsH activity during sporulation
CC (PubMed:9287010). {ECO:0000269|PubMed:17427285,
CC ECO:0000269|PubMed:22463703, ECO:0000269|PubMed:8231808,
CC ECO:0000269|PubMed:9287010}.
CC -!- SUBUNIT: Interacts with SpoIVA (PubMed:17427285). May interact with the
CC ATP-dependent protease FtsH (PubMed:9287010).
CC {ECO:0000269|PubMed:17427285, ECO:0000269|PubMed:9287010}.
CC -!- SUBCELLULAR LOCATION: Forespore outer membrane
CC {ECO:0000269|PubMed:12562810, ECO:0000269|PubMed:17427285,
CC ECO:0000269|PubMed:22463703, ECO:0000269|PubMed:25825747,
CC ECO:0000269|PubMed:29102609}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12562810, ECO:0000269|PubMed:17427285,
CC ECO:0000269|PubMed:25825747}. Note=SpoVM is an atypical amphipathic
CC alpha-helix deeply embedded in the membrane (PubMed:25825747). Proper
CC localization depends on SpoIVA (PubMed:17427285).
CC {ECO:0000269|PubMed:17427285, ECO:0000269|PubMed:25825747}.
CC -!- INDUCTION: Expressed during sporulation and is regulated by the mother
CC cell-specific transcription factors sigma E and SpoIIID
CC (PubMed:8231808). There is a lag-phase of approximately 2 hours between
CC the onset of transcription and translation (PubMed:18820968). The 5'
CC untranslated region negatively influences its own translation
CC (PubMed:18820968). {ECO:0000269|PubMed:18820968,
CC ECO:0000269|PubMed:8231808}.
CC -!- DOMAIN: Residues in the N-terminal region are required for proper
CC localization. {ECO:0000269|PubMed:12562810}.
CC -!- BIOTECHNOLOGY: Nanomolar concentrations inhibit biofilm formation in
CC situ, in S.aureus and in P.aeruginosa, suggesting it might be useful
CC controlling bacterial infections. {ECO:0000269|PubMed:22882210}.
CC -!- MISCELLANEOUS: Preferentially localizes to slightly convex membranes
CC (PubMed:25825747, PubMed:29102609). This preferential adsorption is
CC accurately modeled as a two-step 'dash-and-recruit' mechanism: first,
CC an initial binding event occurs with a faster on rate, then cooperative
CC recruitment of additional SpoVM molecules follows (PubMed:29102609).
CC {ECO:0000269|PubMed:25825747, ECO:0000269|PubMed:29102609}.
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DR EMBL; L12244; AAC36809.1; -; Unassigned_DNA.
DR EMBL; Y13937; CAA74254.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13454.1; -; Genomic_DNA.
DR PIR; S39981; S39981.
DR RefSeq; NP_389463.1; NC_000964.3.
DR RefSeq; WP_003221545.1; NZ_JNCM01000035.1.
DR PDB; 2MVH; NMR; -; A=1-26.
DR PDB; 2MVJ; NMR; -; A=1-26.
DR PDBsum; 2MVH; -.
DR PDBsum; 2MVJ; -.
DR AlphaFoldDB; P37817; -.
DR BMRB; P37817; -.
DR SMR; P37817; -.
DR STRING; 224308.BSU15810; -.
DR PaxDb; P37817; -.
DR EnsemblBacteria; CAB13454; CAB13454; BSU_15810.
DR GeneID; 56671447; -.
DR GeneID; 64303472; -.
DR GeneID; 66216187; -.
DR GeneID; 937168; -.
DR KEGG; bsu:BSU15810; -.
DR PATRIC; fig|224308.179.peg.1721; -.
DR BioCyc; BSUB:BSU15810-MON; -.
DR PRO; PR:P37817; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR012609; Spore_V_M.
DR Pfam; PF08183; SpoV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Reference proteome; Sporulation.
FT CHAIN 1..26
FT /note="Stage V sporulation protein M"
FT /id="PRO_0000072085"
FT REGION 3..9
FT /note="Important for localization"
FT /evidence="ECO:0000269|PubMed:12562810"
FT MUTAGEN 2
FT /note="K->A: Strongly impairs sporulation, but does not
FT affect localization."
FT /evidence="ECO:0000269|PubMed:12562810"
FT MUTAGEN 3
FT /note="F->A: Causes mislocalization and strongly impairs
FT sporulation. Does not affect membrane association."
FT /evidence="ECO:0000269|PubMed:12562810"
FT MUTAGEN 4
FT /note="Y->A: Strongly impairs sporulation, but does not
FT affect localization."
FT /evidence="ECO:0000269|PubMed:12562810"
FT MUTAGEN 6
FT /note="I->A: Causes mislocalization and strongly impairs
FT sporulation. Does not affect membrane association."
FT /evidence="ECO:0000269|PubMed:12562810"
FT MUTAGEN 8
FT /note="L->A: Strongly impairs sporulation, but does not
FT affect localization."
FT /evidence="ECO:0000269|PubMed:12562810"
FT MUTAGEN 9
FT /note="P->A: Causes mislocalization and strongly impairs
FT sporulation. Does not affect membrane association."
FT /evidence="ECO:0000269|PubMed:12562810"
FT MUTAGEN 9
FT /note="P->G: Slightly affects localization and
FT sporulation."
FT /evidence="ECO:0000269|PubMed:29102609"
FT MUTAGEN 12
FT /note="L->A: Strongly impairs sporulation, but does not
FT affect localization."
FT /evidence="ECO:0000269|PubMed:12562810"
FT MUTAGEN 15
FT /note="I->A: Specifically impairs cortex assembly, but not
FT the initiation of coat assembly. Strongly impairs
FT sporulation, but does not affect localization."
FT /evidence="ECO:0000269|PubMed:12562810,
FT ECO:0000269|PubMed:22463703"
FT MUTAGEN 17
FT /note="R->A: Does not affect localization or sporulation."
FT /evidence="ECO:0000269|PubMed:12562810"
FT MUTAGEN 17
FT /note="R->D: Localizes to the mother cell cytosol."
FT /evidence="ECO:0000269|PubMed:25825747"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:2MVH"
SQ SEQUENCE 26 AA; 3018 MW; AC1BD750FCD420D5 CRC64;
MKFYTIKLPK FLGGIVRAML GSFRKD
