(data stored in SCRATCH zone)

SWISSPROT: SP2AB_BACSU

ID   SP2AB_BACSU             Reviewed;         146 AA.
AC   P10728;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   11-DEC-2019, entry version 133.
DE   RecName: Full=Anti-sigma F factor;
DE            EC=2.7.11.1;
DE   AltName: Full=Stage II sporulation protein AB;
GN   Name=spoIIAB; OrderedLocusNames=BSU23460;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   FUNCTION.
RX   PubMed=8460142; DOI=10.1073/pnas.90.6.2325;
RA   Duncan L., Losick R.;
RT   "SpoIIAB is an anti-sigma factor that binds to and inhibits transcription
RT   by regulatory protein sigma F from Bacillus subtilis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:2325-2329(1993).
RN   [5]
RP   FUNCTION, AND PROTEIN SEQUENCE OF 1-14.
RC   STRAIN=CU267;
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).
CC   -!- FUNCTION: Binds to sigma F and blocks its ability to form an RNA
CC       polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine
CC       residue. This phosphorylation may enable SpoIIAA to act as an anti-
CC       anti-sigma factor that counteracts SpoIIAB and thus releases sigma F
CC       from inhibition. {ECO:0000269|PubMed:8358793,
CC       ECO:0000269|PubMed:8460142}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- INTERACTION:
CC       O31435:ybdM; NbExp=2; IntAct=EBI-9344705, EBI-5255200;
CC   -!- DEVELOPMENTAL STAGE: Interaction with SpoIIAB inhibits sigma F activity
CC       throughout the cell before the formation of the asymmetric septum;
CC       after septation the interaction is confined to the mother cell, and
CC       sigma F activity is released in the prespore.
CC   -!- SIMILARITY: Belongs to the anti-sigma-factor family. {ECO:0000305}.
DR   EMBL; M17643; AAA22790.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12654.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14278.1; -; Genomic_DNA.
DR   PIR; B55646; B55646.
DR   RefSeq; NP_390227.1; NC_000964.3.
DR   RefSeq; WP_003230452.1; NZ_JNCM01000036.1.
DR   SMR; P10728; -.
DR   IntAct; P10728; 5.
DR   STRING; 224308.BSU23460; -.
DR   PaxDb; P10728; -.
DR   PRIDE; P10728; -.
DR   EnsemblBacteria; CAB14278; CAB14278; BSU23460.
DR   GeneID; 938930; -.
DR   KEGG; bsu:BSU23460; -.
DR   PATRIC; fig|224308.179.peg.2556; -.
DR   eggNOG; ENOG4108ZBE; Bacteria.
DR   eggNOG; COG2172; LUCA.
DR   HOGENOM; HOG000269931; -.
DR   InParanoid; P10728; -.
DR   KO; K06379; -.
DR   OMA; HAYEDKI; -.
DR   PhylomeDB; P10728; -.
DR   BioCyc; BSUB:BSU23460-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016989; F:sigma factor antagonist activity; IEA:InterPro.
DR   GO; GO:0030436; P:asexual sporulation; IEA:UniProtKB-UniRule.
DR   GO; GO:0042174; P:negative regulation of sporulation resulting in formation of a cellular spore; IEA:InterPro.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00637; Anti_sigma_F; 1.
DR   InterPro; IPR010194; Anti-sigma_F.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   PANTHER; PTHR35526:SF2; PTHR35526:SF2; 1.
DR   Pfam; PF13581; HATPase_c_2; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR01925; spIIAB; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P10728.
DR   SWISS-2DPAGE; P10728.
KW   ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding;
KW   Reference proteome; Serine/threonine-protein kinase; Sporulation;
KW   Transferase.
FT   CHAIN           1..146
FT                   /note="Anti-sigma F factor"
FT                   /id="PRO_0000203561"
SQ   SEQUENCE   146 AA;  16356 MW;  141A28D41EDEC997 CRC64;
     MKNEMHLEFS ALSQNESFAR VTVASFIAQL DPTMDELTEI KTVVSEAVTN AIIHGYEENC
     EGKVYISVTL EDHVVYMTIR DEGLGITDLE EARQPLFTTK PELERSGMGF TIMENFMDDV
     SIDSSPEMGT TIRLTKHLSK SKALCN
//

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