(data stored in ACNUC7421 zone)

SWISSPROT: FIN_BACSU

ID   FIN_BACSU               Reviewed;          76 AA.
AC   P37553;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   11-DEC-2019, entry version 95.
DE   RecName: Full=Anti-sigma-F factor Fin {ECO:0000303|PubMed:21037003};
DE   AltName: Full=Suppressor of recU and recB SubA {ECO:0000303|PubMed:11810266};
GN   Name=fin {ECO:0000303|PubMed:21037003};
GN   Synonyms=subA {ECO:0000303|PubMed:11810266}, yabK;
GN   OrderedLocusNames=BSU00540;
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;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
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   DISRUPTION PHENOTYPE.
RC   STRAIN=168 / YB886 / BG214;
RX   PubMed=11810266; DOI=10.1007/s00438-001-0616-7;
RA   Carrasco B., Fernandez S., Asai K., Ogasawara N., Alonso J.C.;
RT   "Effect of the recU suppressors sms and subA on DNA repair and homologous
RT   recombination in Bacillus subtilis.";
RL   Mol. Genet. Genomics 266:899-906(2002).
RN   [4]
RP   FUNCTION IN DNA REPAIR, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / YB886 / BG214;
RX   PubMed=15317759; DOI=10.1128/jb.186.17.5557-5566.2004;
RA   Carrasco B., Cozar M.C., Lurz R., Alonso J.C., Ayora S.;
RT   "Genetic recombination in Bacillus subtilis 168: contribution of Holliday
RT   junction processing functions in chromosome segregation.";
RL   J. Bacteriol. 186:5557-5566(2004).
RN   [5]
RP   FUNCTION, PUTATIVE COFACTOR, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / PY79;
RX   PubMed=21037003; DOI=10.1128/jb.00949-10;
RA   Camp A.H., Wang A.F., Losick R.;
RT   "A small protein required for the switch from {sigma}F to {sigma}G during
RT   sporulation in Bacillus subtilis.";
RL   J. Bacteriol. 193:116-124(2011).
CC   -!- FUNCTION: An anti-sigma factor for sporulation specific sigma-F factor,
CC       by antagonizing sigma-F it allows the switch to sigma-G factor and
CC       progression to the late sporulation development stages
CC       (PubMed:21037003). Might stabilize or process Holliday junction
CC       intermediates, although this may be due to polar effects on the
CC       downstream mfd gene (PubMed:15317759). {ECO:0000269|PubMed:15317759,
CC       ECO:0000269|PubMed:21037003}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000305|PubMed:21037003};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21037003}.
CC   -!- DEVELOPMENTAL STAGE: Diffusely expressed in the forespore throughout
CC       spore development. {ECO:0000269|PubMed:21037003}.
CC   -!- INDUCTION: Induced at 2 hours after sporulation onset as part of the
CC       sigma-F regulon, followed by further induction after 3 hours as part of
CC       the sigma-G regulon; its concentration rises throughout sporulation (at
CC       protein level) (PubMed:21037003). {ECO:0000269|PubMed:21037003}.
CC   -!- DISRUPTION PHENOTYPE: Cells missing this gene prolong the activity of
CC       sigma-F factor and do not fully induce the activity of sigma-G factor;
CC       sporulation efficiency is reduced 50-fold with most spores arresting in
CC       the engulfment stage (III) (PubMed:21037003). About 10-fold increased
CC       sensitivity to DNA damaging agents, 60% reduced chromosomal DNA
CC       transformation; plasmid transformation is unaffected. Partially
CC       suppresses DNA damaging agent sensitivity of recU deletions
CC       (PubMed:11810266). Partially suppresses DNA damaging agent sensitivity
CC       of recU deletions (PubMed:11810266). Partially suppresses DNA repair
CC       and chromosome segregation defects in ruvA and recG mutants cells, but
CC       not in recD or recU mutant cells (PubMed:15317759).
CC       {ECO:0000269|PubMed:11810266, ECO:0000269|PubMed:15317759,
CC       ECO:0000269|PubMed:21037003}.
CC   -!- CAUTION: Recombination phenotypes may be due to polar effects on the
CC       downstream gene mfd rather than due to loss of the anti-sigma factor
CC       (PubMed:21037003). {ECO:0000305|PubMed:21037003}.
DR   EMBL; D26185; BAA05289.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11830.1; -; Genomic_DNA.
DR   PIR; S66084; S66084.
DR   RefSeq; NP_387935.1; NC_000964.3.
DR   RefSeq; WP_003243417.1; NZ_JNCM01000028.1.
DR   PDB; 5MSL; NMR; -; A=1-73.
DR   PDBsum; 5MSL; -.
DR   SMR; P37553; -.
DR   STRING; 224308.BSU00540; -.
DR   PaxDb; P37553; -.
DR   PRIDE; P37553; -.
DR   EnsemblBacteria; CAB11830; CAB11830; BSU00540.
DR   GeneID; 936978; -.
DR   KEGG; bsu:BSU00540; -.
DR   PATRIC; fig|224308.179.peg.54; -.
DR   HOGENOM; HOG000082069; -.
DR   OMA; VCRHCRT; -.
DR   BioCyc; BSUB:BSU00540-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:InterPro.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   InterPro; IPR020115; Fin.
DR   Pfam; PF10955; DUF2757; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P37553.
DR   SWISS-2DPAGE; P37553.
KW   3D-structure; Cytoplasm; Metal-binding; Reference proteome; Sporulation;
KW   Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..76
FT                   /note="Anti-sigma-F factor Fin"
FT                   /id="PRO_0000049442"
FT   MOTIF           68..71
FT                   /note="YXXY"
FT                   /evidence="ECO:0000305|PubMed:21037003"
FT   METAL           7
FT                   /note="Zinc"
FT                   /evidence="ECO:0000305|PubMed:21037003"
FT   METAL           10
FT                   /note="Zinc"
FT                   /evidence="ECO:0000305|PubMed:21037003"
FT   METAL           55
FT                   /note="Zinc"
FT                   /evidence="ECO:0000305|PubMed:21037003"
FT   METAL           58
FT                   /note="Zinc"
FT                   /evidence="ECO:0000305|PubMed:21037003"
FT   STRAND          4..7
FT                   /evidence="ECO:0000244|PDB:5MSL"
FT   TURN            8..10
FT                   /evidence="ECO:0000244|PDB:5MSL"
FT   TURN            19..21
FT                   /evidence="ECO:0000244|PDB:5MSL"
FT   STRAND          30..33
FT                   /evidence="ECO:0000244|PDB:5MSL"
FT   HELIX           34..39
FT                   /evidence="ECO:0000244|PDB:5MSL"
FT   STRAND          41..43
FT                   /evidence="ECO:0000244|PDB:5MSL"
FT   STRAND          50..53
FT                   /evidence="ECO:0000244|PDB:5MSL"
FT   HELIX           56..64
FT                   /evidence="ECO:0000244|PDB:5MSL"
FT   TURN            65..67
FT                   /evidence="ECO:0000244|PDB:5MSL"
SQ   SEQUENCE   76 AA;  8848 MW;  BA4E9F3DD2914462 CRC64;
     MALHYYCRHC GVKVGSLESS MVSTDSLGFQ HLTNEERNDM ISYKENGDVH VLTICEDCQE
     ALDRNPHYHE YHTFIQ
//

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