SDA_BACSU
ID SDA_BACSU Reviewed; 52 AA.
AC Q7WY62;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Sporulation inhibitor sda;
DE AltName: Full=Histidine kinase KinA inhibitor;
GN Name=sda; OrderedLocusNames=BSU25690;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP IDENTIFICATION, AND FUNCTION.
RC STRAIN=168 / JH642;
RX PubMed=11207367; DOI=10.1016/s0092-8674(01)00211-2;
RA Burkholder W.F., Kurtser I., Grossman A.D.;
RT "Replication initiation proteins regulate a developmental checkpoint in
RT Bacillus subtilis.";
RL Cell 104:269-279(2001).
RN [3]
RP STRUCTURE BY NMR OF 7-52, FUNCTION, INTERACTION WITH KINA, AND MUTAGENESIS
RP OF MET-25; LEU-27; PHE-31 AND LEU-34.
RX PubMed=15023339; DOI=10.1016/s1097-2765(04)00084-x;
RA Rowland S.L., Burkholder W.F., Cunningham K.A., Maciejewski M.W.,
RA Grossman A.D., King G.F.;
RT "Structure and mechanism of action of Sda, an inhibitor of the histidine
RT kinases that regulate initiation of sporulation in Bacillus subtilis.";
RL Mol. Cell 13:689-701(2004).
CC -!- FUNCTION: Mediates a developmental checkpoint inhibiting initiation of
CC sporulation (by preventing phosphorylation of spo0A) in response to
CC defects in the replication initiation machinery. Inhibits
CC autophosphorylation of the histidine protein kinase KinA, forming a
CC molecular barricade that prevents productive interaction between the
CC ATP-binding site in the catalytic domain and the phosphorylatable His
CC in the phosphotransfer domain of KinA. Probably also inhibits the
CC activity of KinB, but has relatively little effect on KinC. Has at
CC least one target in vivo in addition to KinA as sda does not require
CC KinA to inhibit sporulation. {ECO:0000269|PubMed:11207367,
CC ECO:0000269|PubMed:15023339}.
CC -!- SUBUNIT: Forms a stable heterotetramer with KinA (comprising two
CC molecules of each protein), by binding to the KinA
CC dimerization/phosphotransfer domain.
CC -!- INTERACTION:
CC Q7WY62; P16497: kinA; NbExp=6; IntAct=EBI-6405714, EBI-6405707;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q7WY62-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7WY62-2; Sequence=VSP_018790;
CC -!- MISCELLANEOUS: [Isoform 2]: Seems to be the major isoform.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAE01463.1; -; Genomic_DNA.
DR RefSeq; WP_010886571.1; NC_000964.3.
DR RefSeq; YP_054588.1; NC_000964.3. [Q7WY62-1]
DR PDB; 1PV0; NMR; -; A=7-52.
DR PDB; 3FYR; X-ray; 1.97 A; A/B/C=7-52.
DR PDBsum; 1PV0; -.
DR PDBsum; 3FYR; -.
DR AlphaFoldDB; Q7WY62; -.
DR BMRB; Q7WY62; -.
DR SASBDB; Q7WY62; -.
DR SMR; Q7WY62; -.
DR IntAct; Q7WY62; 1.
DR STRING; 224308.BSU25690; -.
DR PaxDb; Q7WY62; -.
DR PRIDE; Q7WY62; -.
DR EnsemblBacteria; CAE01463; CAE01463; BSU_25690.
DR GeneID; 2914223; -.
DR KEGG; bsu:BSU25690; -.
DR PATRIC; fig|224308.43.peg.2679; -.
DR eggNOG; ENOG5033C8I; Bacteria.
DR OMA; MKCLPDD; -.
DR BioCyc; BSUB:BSU25690-MON; -.
DR EvolutionaryTrace; Q7WY62; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.1100; -; 1.
DR InterPro; IPR015064; Sda.
DR InterPro; IPR036916; Sda_sf.
DR Pfam; PF08970; Sda; 1.
DR SUPFAM; SSF100985; SSF100985; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Protein kinase inhibitor;
KW Reference proteome; Sporulation.
FT CHAIN 1..52
FT /note="Sporulation inhibitor sda"
FT /id="PRO_0000022288"
FT SITE 25
FT /note="Important for interaction with KinA"
FT /evidence="ECO:0000305"
FT SITE 27
FT /note="Important for interaction with KinA"
FT /evidence="ECO:0000305"
FT SITE 31
FT /note="Important for interaction with KinA"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..6
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018790"
FT MUTAGEN 25
FT /note="M->A,I: Partial loss of ability to inhibit KinA
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:15023339"
FT MUTAGEN 27
FT /note="L->A,E: Complete loss of ability to inhibit KinA
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:15023339"
FT MUTAGEN 31
FT /note="F->H: Complete loss of ability to inhibit KinA
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:15023339"
FT MUTAGEN 34
FT /note="L->A: Partial loss of ability to inhibit KinA
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:15023339"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:3FYR"
FT HELIX 29..43
FT /evidence="ECO:0007829|PDB:3FYR"
FT TURN 45..49
FT /evidence="ECO:0007829|PDB:1PV0"
SQ SEQUENCE 52 AA; 6155 MW; BCBDECF0E0203CAE CRC64;
MNWVPSMRKL SDELLIESYF KATEMNLNRD FIELIENEIK RRSLGHIISV SS
