(data stored in SCRATCH zone)

SWISSPROT: SP2AA_BACSU

ID   SP2AA_BACSU             Reviewed;         117 AA.
AC   P10727;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   11-DEC-2019, entry version 150.
DE   RecName: Full=Anti-sigma F factor antagonist;
DE   AltName: Full=Stage II sporulation protein AA;
GN   Name=spoIIAA; OrderedLocusNames=BSU23470;
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=CU267;
RX   PubMed=6088674; DOI=10.1099/00221287-130-8-2147;
RA   Fort P., Piggot P.J.;
RT   "Nucleotide sequence of sporulation locus spoIIA in Bacillus subtilis.";
RL   J. Gen. Microbiol. 130:2147-2153(1984).
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   PROTEIN SEQUENCE OF 2-4.
RX   PubMed=1629150; DOI=10.1128/jb.174.15.4885-4892.1992;
RA   Wu J.-J., Schuch R., Piggot P.J.;
RT   "Characterization of a Bacillus subtilis sporulation operon that includes
RT   genes for an RNA polymerase sigma factor and for a putative DD-
RT   carboxypeptidase.";
RL   J. Bacteriol. 174:4885-4892(1992).
RN   [5]
RP   FUNCTION, AND PROTEIN SEQUENCE OF 2-14.
RX   PubMed=8358793; DOI=10.1016/0092-8674(93)90520-z;
RA   Min K.-T., Hilditch C.M., Diederich B., Errington J., Yudkin M.D.;
RT   "Sigma F, the first compartment-specific transcription factor of B.
RT   subtilis, is regulated by an anti-sigma factor that is also a protein
RT   kinase.";
RL   Cell 74:735-742(1993).
RN   [6]
RP   PHOSPHORYLATION AT SER-58, AND PROTEIN SEQUENCE OF 52-67.
RX   PubMed=7751305; DOI=10.1128/jb.177.10.2912-2913.1995;
RA   Najafi S.M.A., Willis A.C., Yudkin M.D.;
RT   "Site of phosphorylation of SpoIIAA, the anti-anti-sigma factor for
RT   sporulation-specific sigma F of Bacillus subtilis.";
RL   J. Bacteriol. 177:2912-2913(1995).
RN   [7]
RP   STRUCTURE BY NMR.
RX   PubMed=9560229; DOI=10.1073/pnas.95.9.5067;
RA   Kovacs H., Comfort D., Lord M., Campbell I.D., Yudkin M.D.;
RT   "Solution structure of SpoIIAA, a phosphorylatable component of the system
RT   that regulates transcription factor sigmaF of Bacillus subtilis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:5067-5071(1998).
CC   -!- FUNCTION: In the phosphorylated form it could act as an anti-anti-sigma
CC       factor that counteracts SpoIIAB and thus releases sigma f from
CC       inhibition. {ECO:0000269|PubMed:8358793}.
CC   -!- PTM: Phosphorylated by SpoIIAB on a serine residue.
CC       {ECO:0000269|PubMed:7751305}.
CC   -!- SIMILARITY: Belongs to the anti-sigma-factor antagonist family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA22789.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; M17643; AAA22789.1; ALT_INIT; Genomic_DNA.
DR   EMBL; D84432; BAA12653.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14279.1; -; Genomic_DNA.
DR   PIR; A55646; A55646.
DR   RefSeq; NP_390228.1; NC_000964.3.
DR   RefSeq; WP_004398633.1; NZ_JNCM01000036.1.
DR   PDB; 1AUZ; NMR; -; A=2-117.
DR   PDB; 1BUZ; NMR; -; A=2-117.
DR   PDBsum; 1AUZ; -.
DR   PDBsum; 1BUZ; -.
DR   SMR; P10727; -.
DR   IntAct; P10727; 1.
DR   STRING; 224308.BSU23470; -.
DR   iPTMnet; P10727; -.
DR   jPOST; P10727; -.
DR   PaxDb; P10727; -.
DR   PRIDE; P10727; -.
DR   EnsemblBacteria; CAB14279; CAB14279; BSU23470.
DR   GeneID; 938730; -.
DR   KEGG; bsu:BSU23470; -.
DR   PATRIC; fig|224308.179.peg.2557; -.
DR   eggNOG; ENOG41082AN; Bacteria.
DR   eggNOG; COG1366; LUCA.
DR   HOGENOM; HOG000270156; -.
DR   InParanoid; P10727; -.
DR   KO; K06378; -.
DR   OMA; SYFKMFN; -.
DR   PhylomeDB; P10727; -.
DR   BioCyc; BSUB:BSU23470-MONOMER; -.
DR   EvolutionaryTrace; P10727; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0043856; F:anti-sigma factor antagonist activity; IBA:GO_Central.
DR   GO; GO:0045152; F:antisigma factor binding; IEA:InterPro.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.750.24; -; 1.
DR   InterPro; IPR003658; Anti-sigma_ant.
DR   InterPro; IPR014237; Anti-sigma_F_ant.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   Pfam; PF01740; STAS; 1.
DR   SUPFAM; SSF52091; SSF52091; 1.
DR   TIGRFAMs; TIGR00377; ant_ant_sig; 1.
DR   TIGRFAMs; TIGR02886; spore_II_AA; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P10727.
DR   SWISS-2DPAGE; P10727.
KW   3D-structure; Direct protein sequencing; Phosphoprotein;
KW   Reference proteome; Sporulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1629150,
FT                   ECO:0000269|PubMed:8358793"
FT   CHAIN           2..117
FT                   /note="Anti-sigma F factor antagonist"
FT                   /id="PRO_0000194204"
FT   DOMAIN          3..113
FT                   /note="STAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT   MOD_RES         58
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:7751305"
FT   STRAND          7..10
FT                   /evidence="ECO:0000244|PDB:1AUZ"
FT   STRAND          13..16
FT                   /evidence="ECO:0000244|PDB:1AUZ"
FT   HELIX           26..38
FT                   /evidence="ECO:0000244|PDB:1AUZ"
FT   STRAND          45..49
FT                   /evidence="ECO:0000244|PDB:1AUZ"
FT   HELIX           60..74
FT                   /evidence="ECO:0000244|PDB:1AUZ"
FT   TURN            85..88
FT                   /evidence="ECO:0000244|PDB:1AUZ"
FT   HELIX           89..94
FT                   /evidence="ECO:0000244|PDB:1AUZ"
FT   HELIX           97..99
FT                   /evidence="ECO:0000244|PDB:1AUZ"
FT   HELIX           106..108
FT                   /evidence="ECO:0000244|PDB:1AUZ"
FT   HELIX           110..112
FT                   /evidence="ECO:0000244|PDB:1AUZ"
SQ   SEQUENCE   117 AA;  12990 MW;  2333E74207568AC2 CRC64;
     MSLGIDMNVK ESVLCIRLTG ELDHHTAETL KQKVTQSLEK DDIRHIVLNL EDLSFMDSSG
     LGVILGRYKQ IKQIGGEMVV CAISPAVKRL FDMSGLFKII RFEQSEQQAL LTLGVAS
//

If you have problems or comments...

PBIL Back to PBIL home page