SP2SA_BACSU
ID SP2SA_BACSU Reviewed; 248 AA.
AC O34853;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Stage II sporulation protein SA;
DE AltName: Full=Killer protein SpoIISA;
DE AltName: Full=Toxin SpoIISA;
GN Name=spoIISA; Synonyms=ykaC; OrderedLocusNames=BSU12830;
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;
RA Devine K.M.;
RT "Sequence of the Bacillus subtilis genome between xlyA and ykoR.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
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 AS A TOXIN, SUBUNIT, MUTAGENESIS OF ARG-38 AND LEU-103, INDUCTION,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / JH642;
RX PubMed=11371520; DOI=10.1128/jb.183.12.3574-3581.2001;
RA Adler E., Barak I., Stragier P.;
RT "Bacillus subtilis locus encoding a killer protein and its antidote.";
RL J. Bacteriol. 183:3574-3581(2001).
RN [4]
RP EXPRESSION IN E.COLI.
RC STRAIN=168 / JH642;
RX PubMed=18096016; DOI=10.1111/j.1574-6968.2007.00984.x;
RA Florek P., Muchova K., Pavelcikova P., Barak I.;
RT "Expression of functional Bacillus SpoIISAB toxin-antitoxin modules in
RT Escherichia coli.";
RL FEMS Microbiol. Lett. 278:177-184(2008).
RN [5]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=168 / PY79;
RX PubMed=20863891; DOI=10.1016/j.resmic.2010.09.005;
RA Resetarova S., Florek P., Muchova K., Wilkinson A.J., Barak I.;
RT "Expression and localization of SpoIISA toxin during the life cycle of
RT Bacillus subtilis.";
RL Res. Microbiol. 161:750-756(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 92-248, AND INTERACTION WITH
RP SPOIISB.
RC STRAIN=168 / PY79;
RX PubMed=21147767; DOI=10.1074/jbc.m110.172429;
RA Florek P., Levdikov V.M., Blagova E., Lebedev A.A., Skrabana R.,
RA Resetarova S., Pavelcikova P., Barak I., Wilkinson A.J.;
RT "The structure and interactions of SpoIISA and SpoIISB, a toxin-antitoxin
RT system in Bacillus subtilis.";
RL J. Biol. Chem. 286:6808-6819(2011).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Its
CC toxic activity is neutralized by cognate antitoxin SpoIISB. Expression
CC in the absence of SpoIISB permits sporulation to stage II, when
CC plasmolysis zones and holes in the peptidoglycan layer are observed,
CC resulting in cell death. Lethal when synthesized during vegetative
CC growth in the absence of SpoIISB. In E.coli both the membrane bound and
CC soluble domain are required in cis for toxin activity.
CC {ECO:0000269|PubMed:11371520}.
CC -!- SUBUNIT: Probably forms an oligomer; X-ray data suggests the inactive
CC complex forms a heterotetramer of SpoIISA(2)-SpoIISB(2), which
CC inactivates the toxic activity of SpoIISA.
CC {ECO:0000269|PubMed:11371520}.
CC -!- INTERACTION:
CC O34853; O34800: spoIISB; NbExp=3; IntAct=EBI-4406150, EBI-4406141;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20863891};
CC Multi-pass membrane protein {ECO:0000269|PubMed:20863891}.
CC -!- INDUCTION: Expressed at low levels during exponential growth, it
CC increases dramatically at the onset of sporulation (at protein level).
CC A member of the spoIISA-spoIISB operon. {ECO:0000269|PubMed:11371520,
CC ECO:0000269|PubMed:20863891}.
CC -!- DISRUPTION PHENOTYPE: No change in sporulation efficiency.
CC {ECO:0000269|PubMed:11371520}.
CC -!- SIMILARITY: Belongs to the SpoIISA toxin family. {ECO:0000305}.
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DR EMBL; AJ002571; CAA05563.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13140.1; -; Genomic_DNA.
DR PIR; D69713; D69713.
DR RefSeq; NP_389166.1; NC_000964.3.
DR RefSeq; WP_003244695.1; NZ_JNCM01000035.1.
DR PDB; 3O6Q; X-ray; 2.50 A; A/C=92-248.
DR PDBsum; 3O6Q; -.
DR AlphaFoldDB; O34853; -.
DR SMR; O34853; -.
DR IntAct; O34853; 1.
DR STRING; 224308.BSU12830; -.
DR TCDB; 9.A.10.1.1; the oligomeric probable pore-forming spoiia toxin (spoiia) family.
DR PaxDb; O34853; -.
DR PRIDE; O34853; -.
DR EnsemblBacteria; CAB13140; CAB13140; BSU_12830.
DR GeneID; 938174; -.
DR KEGG; bsu:BSU12830; -.
DR PATRIC; fig|224308.179.peg.1392; -.
DR eggNOG; ENOG5033VU0; Bacteria.
DR OMA; AIRKTWY; -.
DR BioCyc; BSUB:BSU12830-MON; -.
DR Proteomes; UP000001570; Chromosome.
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:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR025940; SpoIISA_toxin.
DR Pfam; PF14171; SpoIISA_toxin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Reference proteome; Sporulation;
KW Toxin-antitoxin system; Transmembrane; Transmembrane helix.
FT CHAIN 1..248
FT /note="Stage II sporulation protein SA"
FT /id="PRO_0000072062"
FT TOPO_DOM 1..3
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 22..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..67
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 38
FT /note="R->Q: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:11371520"
FT MUTAGEN 103
FT /note="L->F: In mut9; sporulation efficiency decreases by
FT about 4 orders of magnitude."
FT /evidence="ECO:0000269|PubMed:11371520"
FT HELIX 98..126
FT /evidence="ECO:0007829|PDB:3O6Q"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:3O6Q"
FT HELIX 136..152
FT /evidence="ECO:0007829|PDB:3O6Q"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:3O6Q"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:3O6Q"
FT HELIX 166..173
FT /evidence="ECO:0007829|PDB:3O6Q"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:3O6Q"
FT STRAND 197..206
FT /evidence="ECO:0007829|PDB:3O6Q"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:3O6Q"
FT HELIX 223..239
FT /evidence="ECO:0007829|PDB:3O6Q"
SQ SEQUENCE 248 AA; 29061 MW; 16E9CA02AEAF2F6D CRC64;
MVLFFQIMVW CIVAGLGLYV YATWRFEAKV KEKMSAIRKT WYLLFVLGAM VYWTYEPTSL
FTHWERYLIV AVSFALIDAF IFLSAYVKKL AGSELETDTR EILEENNEML HMYLNRLKTY
QYLLKNEPIH VYYGSIDAYA EGIDKLLKTY ADKMNLTASL CHYSTQADKD RLTEHMDDPA
DVQTRLDRKD VYYDQYGKVV LIPFTIETQN YVIKLTSDSI VTEFDYLLFT SLTSIYDLVL
PIEEEGEG
