(data stored in SCRATCH zone)

SWISSPROT: GIN_BACSU

ID   GIN_BACSU               Reviewed;          64 AA.
AC   P37534;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   11-DEC-2019, entry version 88.
DE   RecName: Full=Anti-sigma-G factor Gin {ECO:0000303|PubMed:18208527};
DE   AltName: Full=Protein CsfB {ECO:0000303|PubMed:8759874};
GN   Name=csfB {ECO:0000303|PubMed:8759874};
GN   Synonyms=gin {ECO:0000303|PubMed:18208527}, yaaM;
GN   OrderedLocusNames=BSU00240;
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   Bookstein C., Edwards C.W., Hulett F.M.;
RT   "Characterization of the Bacillus subtilis xpaC gene, which in double copy
RT   causes aberrant cell morphology, filamentation and inhibits sporulation.";
RL   Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [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   DEVELOPMENTAL STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / PY79;
RX   PubMed=8759874; DOI=10.1128/jb.178.16.5039-5041.1996;
RA   Decatur A., Losick R.;
RT   "Identification of additional genes under the control of the transcription
RT   factor sigma F of Bacillus subtilis.";
RL   J. Bacteriol. 178:5039-5041(1996).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / BR151;
RX   PubMed=17921305; DOI=10.1128/jb.01265-07;
RA   Chary V.K., Xenopoulos P., Piggot P.J.;
RT   "Expression of the sigmaF-directed csfB locus prevents premature appearance
RT   of sigmaG activity during sporulation of Bacillus subtilis.";
RL   J. Bacteriol. 189:8754-8757(2007).
RN   [6]
RP   FUNCTION, INTERACTION WITH SIGMA-G FACTOR, AND MUTAGENESIS OF
RP   15-ASP--ASP-32.
RC   STRAIN=168 / JH642;
RX   PubMed=18208527; DOI=10.1111/j.1365-2958.2008.06121.x;
RA   Karmazyn-Campelli C., Rhayat L., Carballido-Lopez R., Duperrier S.,
RA   Frandsen N., Stragier P.;
RT   "How the early sporulation sigma factor sigmaF delays the switch to late
RT   development in Bacillus subtilis.";
RL   Mol. Microbiol. 67:1169-1180(2008).
RN   [7]
RP   FUNCTION, INTERACTION WITH SIGMA-G FACTOR, AND MUTAGENESIS OF
RP   11-CYS--CYS-14; CYS-11; CYS-14; GLY-21; 30-CYS--CYS-33; CYS-30; CYS-33;
RP   TYR-47; 49-PHE-TYR-50; TYR-50 AND VAL-51.
RX   PubMed=19497328; DOI=10.1016/j.jmb.2009.05.073;
RA   Rhayat L., Duperrier S., Carballido-Lopez R., Pellegrini O., Stragier P.;
RT   "Genetic dissection of an inhibitor of the sporulation sigma factor
RT   sigma(G).";
RL   J. Mol. Biol. 390:835-844(2009).
CC   -!- FUNCTION: An anti-sigma-G factor, prevents premature activation of
CC       sigma-G factor in the forespore; overexpression leads to 1000-fold
CC       reduction in spore formation, spore formation stops after engulfment
CC       (PubMed:17921305, PubMed:19497328). Overexpression also inhibits sigma-
CC       G transcription activation activity (PubMed:18208527). When both Gin
CC       and sigma-G are expressed in E.coli Gin inhibits sigma-G, strongly
CC       suggesting Gin inhibits by direct physical interaction
CC       (PubMed:19497328). {ECO:0000269|PubMed:17921305,
CC       ECO:0000269|PubMed:18208527, ECO:0000269|PubMed:19497328}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:19497328};
CC       Note=Binds 0.5 mol of zinc/mol protein, probably 1 zinc per dimer.
CC       {ECO:0000269|PubMed:19497328};
CC   -!- SUBUNIT: Probably functions as a homodimer (PubMed:19497328). Interacts
CC       with sigma-G factor, recognition occurs via the first 71 residues of
CC       sigma-G (PubMed:18208527, PubMed:19497328).
CC       {ECO:0000269|PubMed:18208527, ECO:0000269|PubMed:19497328}.
CC   -!- DEVELOPMENTAL STAGE: Expressed starting 2 hours after sporulation onset
CC       for at least 7 hours. {ECO:0000269|PubMed:8759874}.
CC   -!- INDUCTION: During sporulation under control of sigma-F factor.
CC       {ECO:0000269|PubMed:8759874}.
CC   -!- DISRUPTION PHENOTYPE: Premature expression of sigma-G factor (sigG or
CC       spoIIIG) activity during the early stages of forespore development
CC       (PubMed:17921305, PubMed:18208527). Spore formation continues normally
CC       (PubMed:17921305, PubMed:8759874). However its absence has deleterious
CC       effects on strain robustness and is strongly selected against in
CC       competitions experiments (PubMed:18208527).
CC       {ECO:0000269|PubMed:17921305, ECO:0000269|PubMed:18208527,
CC       ECO:0000269|PubMed:8759874}.
DR   EMBL; M96156; AAA22890.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05260.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11800.1; -; Genomic_DNA.
DR   PIR; S27525; S27525.
DR   RefSeq; NP_387905.1; NC_000964.3.
DR   RefSeq; WP_003243294.1; NZ_JNCM01000028.1.
DR   PDB; 5N7Y; NMR; -; A/C=1-48.
DR   PDBsum; 5N7Y; -.
DR   SMR; P37534; -.
DR   STRING; 224308.BSU00240; -.
DR   PaxDb; P37534; -.
DR   PRIDE; P37534; -.
DR   EnsemblBacteria; CAB11800; CAB11800; BSU00240.
DR   GeneID; 937016; -.
DR   KEGG; bsu:BSU00240; -.
DR   PATRIC; fig|224308.179.peg.24; -.
DR   HOGENOM; HOG000262411; -.
DR   OMA; DAKYHFF; -.
DR   BioCyc; BSUB:BSU00240-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   InterPro; IPR019700; Sigma-G_inhibitor_Gin.
DR   Pfam; PF10764; Gin; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P37534.
DR   SWISS-2DPAGE; P37534.
KW   3D-structure; Metal-binding; Reference proteome; Sporulation;
KW   Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..64
FT                   /note="Anti-sigma-G factor Gin"
FT                   /id="PRO_0000079393"
FT   METAL           11
FT                   /note="Zinc"
FT                   /evidence="ECO:0000305|PubMed:19497328"
FT   METAL           14
FT                   /note="Zinc"
FT                   /evidence="ECO:0000305|PubMed:19497328"
FT   METAL           30
FT                   /note="Zinc"
FT                   /evidence="ECO:0000305|PubMed:19497328"
FT   METAL           33
FT                   /note="Zinc"
FT                   /evidence="ECO:0000305|PubMed:19497328"
FT   MUTAGEN         11..14
FT                   /note="CVIC->AVIA: No longer inhibits sigma-G. Restores 70%
FT                   of sigma-G inhibition; when associated with 30-A--A-33."
FT                   /evidence="ECO:0000269|PubMed:19497328"
FT   MUTAGEN         11
FT                   /note="C->A: No longer inhibits sigma-G."
FT                   /evidence="ECO:0000269|PubMed:19497328"
FT   MUTAGEN         14
FT                   /note="C->A: No longer inhibits or interacts with sigma-G."
FT                   /evidence="ECO:0000269|PubMed:19497328"
FT   MUTAGEN         15..32
FT                   /note="DQEKNRGIHLYTKFICLD->RKPLKDGIIINGKGICKS: Loss of most
FT                   ability to inhibit sigma-G, no longer interacts with sigma-
FT                   G, replace sequence with same region from
FT                   C.acetobutylicum."
FT                   /evidence="ECO:0000269|PubMed:18208527"
FT   MUTAGEN         21
FT                   /note="G->C: Loss of most sigma-G inhibition."
FT                   /evidence="ECO:0000269|PubMed:19497328"
FT   MUTAGEN         30..33
FT                   /note="CLDC->ALDA: No longer inhibits sigma-G. Restores 70%
FT                   of sigma-G inhibition; when associated with 11-A--A-14."
FT                   /evidence="ECO:0000269|PubMed:19497328"
FT   MUTAGEN         30
FT                   /note="C->A: No longer inhibits sigma-G."
FT                   /evidence="ECO:0000269|PubMed:19497328"
FT   MUTAGEN         33
FT                   /note="C->A: No longer inhibits or interacts with sigma-G."
FT                   /evidence="ECO:0000269|PubMed:19497328"
FT   MUTAGEN         47
FT                   /note="Y->A: No longer inhibits or interacts with sigma-G."
FT                   /evidence="ECO:0000269|PubMed:19497328"
FT   MUTAGEN         49..50
FT                   /note="FY->AA: No longer inhibits sigma-G, still slight
FT                   interaction with sigma-G."
FT                   /evidence="ECO:0000269|PubMed:19497328"
FT   MUTAGEN         50
FT                   /note="Y->A: Partial loss of sigma-G inhibition."
FT                   /evidence="ECO:0000269|PubMed:19497328"
FT   MUTAGEN         51
FT                   /note="V->A: Loss of most sigma-G inhibition, still slight
FT                   interaction with sigma-G."
FT                   /evidence="ECO:0000269|PubMed:19497328"
FT   STRAND          7..10
FT                   /evidence="ECO:0000244|PDB:5N7Y"
FT   TURN            12..14
FT                   /evidence="ECO:0000244|PDB:5N7Y"
FT   STRAND          17..22
FT                   /evidence="ECO:0000244|PDB:5N7Y"
FT   STRAND          24..26
FT                   /evidence="ECO:0000244|PDB:5N7Y"
FT   HELIX           31..40
FT                   /evidence="ECO:0000244|PDB:5N7Y"
SQ   SEQUENCE   64 AA;  7439 MW;  C423AA65E835E8F5 CRC64;
     MDETVKLNHT CVICDQEKNR GIHLYTKFIC LDCERKVIST STSDPDYAFY VKKLKSIHTP
     PLYS
//

If you have problems or comments...

PBIL Back to PBIL home page