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Anti-sigma-G factor Gin (Protein CsfB)

 GIN_BACSU               Reviewed;          64 AA.
P37534;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 1.
23-MAY-2018, entry version 84.
RecName: Full=Anti-sigma-G factor Gin {ECO:0000303|PubMed:18208527};
AltName: Full=Protein CsfB {ECO:0000303|PubMed:8759874};
Name=csfB {ECO:0000303|PubMed:8759874};
Synonyms=gin {ECO:0000303|PubMed:18208527}, yaaM;
OrderedLocusNames=BSU00240;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
Bookstein C., Edwards C.W., Hulett F.M.;
"Characterization of the Bacillus subtilis xpaC gene, which in double
copy causes aberrant cell morphology, filamentation and inhibits
sporulation.";
Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=7584024; DOI=10.1093/dnares/1.1.1;
Ogasawara N., Nakai S., Yoshikawa H.;
"Systematic sequencing of the 180 kilobase region of the Bacillus
subtilis chromosome containing the replication origin.";
DNA Res. 1:1-14(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[4]
DEVELOPMENTAL STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=168 / PY79;
PubMed=8759874; DOI=10.1128/jb.178.16.5039-5041.1996;
Decatur A., Losick R.;
"Identification of additional genes under the control of the
transcription factor sigma F of Bacillus subtilis.";
J. Bacteriol. 178:5039-5041(1996).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=168 / BR151;
PubMed=17921305; DOI=10.1128/JB.01265-07;
Chary V.K., Xenopoulos P., Piggot P.J.;
"Expression of the sigmaF-directed csfB locus prevents premature
appearance of sigmaG activity during sporulation of Bacillus
subtilis.";
J. Bacteriol. 189:8754-8757(2007).
[6]
FUNCTION, INTERACTION WITH SIGMA-G FACTOR, AND MUTAGENESIS OF
15-ASP--ASP-32.
STRAIN=168 / JH642;
PubMed=18208527; DOI=10.1111/j.1365-2958.2008.06121.x;
Karmazyn-Campelli C., Rhayat L., Carballido-Lopez R., Duperrier S.,
Frandsen N., Stragier P.;
"How the early sporulation sigma factor sigmaF delays the switch to
late development in Bacillus subtilis.";
Mol. Microbiol. 67:1169-1180(2008).
[7]
FUNCTION, INTERACTION WITH SIGMA-G FACTOR, AND MUTAGENESIS OF
11-CYS--CYS-14; CYS-11; CYS-14; GLY-21; 30-CYS--CYS-33; CYS-30;
CYS-33; TYR-47; 49-PHE-TYR-50; TYR-50 AND VAL-51.
PubMed=19497328; DOI=10.1016/j.jmb.2009.05.073;
Rhayat L., Duperrier S., Carballido-Lopez R., Pellegrini O.,
Stragier P.;
"Genetic dissection of an inhibitor of the sporulation sigma factor
sigma(G).";
J. Mol. Biol. 390:835-844(2009).
-!- FUNCTION: An anti-sigma-G factor, prevents premature activation of
sigma-G factor in the forespore; overexpression leads to 1000-fold
reduction in spore formation, spore formation stops after
engulfment (PubMed:17921305, PubMed:19497328). Overexpression also
inhibits sigma-G transcription activation activity
(PubMed:18208527). When both Gin and sigma-G are expressed in
E.coli Gin inhibits sigma-G, strongly suggesting Gin inhibits by
direct physical interaction (PubMed:19497328).
{ECO:0000269|PubMed:17921305, ECO:0000269|PubMed:18208527,
ECO:0000269|PubMed:19497328}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:19497328};
Note=Binds 0.5 mol of zinc/mol protein, probably 1 zinc per dimer.
{ECO:0000269|PubMed:19497328};
-!- SUBUNIT: Probably functions as a homodimer (PubMed:19497328).
Interacts with sigma-G factor, recognition occurs via the first 71
residues of sigma-G (PubMed:18208527, PubMed:19497328).
{ECO:0000269|PubMed:18208527, ECO:0000269|PubMed:19497328}.
-!- DEVELOPMENTAL STAGE: Expressed starting 2 hours after sporulation
onset for at least 7 hours. {ECO:0000269|PubMed:8759874}.
-!- INDUCTION: During sporulation under control of sigma-F factor.
{ECO:0000269|PubMed:8759874}.
-!- DISRUPTION PHENOTYPE: Premature expression of sigma-G factor (sigG
or spoIIIG) activity during the early stages of forespore
development (PubMed:17921305, PubMed:18208527). Spore formation
continues normally (PubMed:17921305, PubMed:8759874). However its
absence has deleterious effects on strain robustness and is
strongly selected against in competitions experiments
(PubMed:18208527). {ECO:0000269|PubMed:17921305,
ECO:0000269|PubMed:18208527, ECO:0000269|PubMed:8759874}.
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EMBL; M96156; AAA22890.1; -; Genomic_DNA.
EMBL; D26185; BAA05260.1; -; Genomic_DNA.
EMBL; AL009126; CAB11800.1; -; Genomic_DNA.
PIR; S27525; S27525.
RefSeq; NP_387905.1; NC_000964.3.
RefSeq; WP_003243294.1; NZ_JNCM01000028.1.
PDB; 5N7Y; NMR; -; A/C=1-48.
PDBsum; 5N7Y; -.
SMR; P37534; -.
STRING; 224308.Bsubs1_010100000120; -.
PaxDb; P37534; -.
PRIDE; P37534; -.
EnsemblBacteria; CAB11800; CAB11800; BSU00240.
GeneID; 937016; -.
KEGG; bsu:BSU00240; -.
PATRIC; fig|224308.179.peg.24; -.
HOGENOM; HOG000262411; -.
OMA; DAKYHFF; -.
BioCyc; BSUB:BSU00240-MONOMER; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR019700; Sigma-G_inhibitor_Gin.
Pfam; PF10764; Gin; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Metal-binding; Reference proteome;
Sporulation; Transcription; Transcription regulation; Zinc.
CHAIN 1 64 Anti-sigma-G factor Gin.
/FTId=PRO_0000079393.
METAL 11 11 Zinc. {ECO:0000305|PubMed:19497328}.
METAL 14 14 Zinc. {ECO:0000305|PubMed:19497328}.
METAL 30 30 Zinc. {ECO:0000305|PubMed:19497328}.
METAL 33 33 Zinc. {ECO:0000305|PubMed:19497328}.
MUTAGEN 11 14 CVIC->AVIA: No longer inhibits sigma-G.
Restores 70% of sigma-G inhibition; when
associated with 30-A--A-33.
{ECO:0000269|PubMed:19497328}.
MUTAGEN 11 11 C->A: No longer inhibits sigma-G.
{ECO:0000269|PubMed:19497328}.
MUTAGEN 14 14 C->A: No longer inhibits or interacts
with sigma-G.
{ECO:0000269|PubMed:19497328}.
MUTAGEN 15 32 DQEKNRGIHLYTKFICLD->RKPLKDGIIINGKGICKS:
Loss of most ability to inhibit sigma-G,
no longer interacts with sigma-G, replace
sequence with same region from
C.acetobutylicum.
{ECO:0000269|PubMed:18208527}.
MUTAGEN 21 21 G->C: Loss of most sigma-G inhibition.
{ECO:0000269|PubMed:19497328}.
MUTAGEN 30 33 CLDC->ALDA: No longer inhibits sigma-G.
Restores 70% of sigma-G inhibition; when
associated with 11-A--A-14.
{ECO:0000269|PubMed:19497328}.
MUTAGEN 30 30 C->A: No longer inhibits sigma-G.
{ECO:0000269|PubMed:19497328}.
MUTAGEN 33 33 C->A: No longer inhibits or interacts
with sigma-G.
{ECO:0000269|PubMed:19497328}.
MUTAGEN 47 47 Y->A: No longer inhibits or interacts
with sigma-G.
{ECO:0000269|PubMed:19497328}.
MUTAGEN 49 50 FY->AA: No longer inhibits sigma-G, still
slight interaction with sigma-G.
{ECO:0000269|PubMed:19497328}.
MUTAGEN 50 50 Y->A: Partial loss of sigma-G inhibition.
{ECO:0000269|PubMed:19497328}.
MUTAGEN 51 51 V->A: Loss of most sigma-G inhibition,
still slight interaction with sigma-G.
{ECO:0000269|PubMed:19497328}.
STRAND 7 10 {ECO:0000244|PDB:5N7Y}.
TURN 12 14 {ECO:0000244|PDB:5N7Y}.
STRAND 17 22 {ECO:0000244|PDB:5N7Y}.
STRAND 24 26 {ECO:0000244|PDB:5N7Y}.
HELIX 31 40 {ECO:0000244|PDB:5N7Y}.
SEQUENCE 64 AA; 7439 MW; C423AA65E835E8F5 CRC64;
MDETVKLNHT CVICDQEKNR GIHLYTKFIC LDCERKVIST STSDPDYAFY VKKLKSIHTP
PLYS


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