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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.
10-APR-2019, entry version 86.
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.BSU00240; -.
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:0030435; P:sporulation resulting in formation of a cellular spore; 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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[rsrA SCO5217] Anti-sigma factor RsrA (Regulator of SigR) (Sigma-R anti-sigma factor RsrA)
[rslA Rv0736] Anti-sigma-L factor RslA (Regulator of SigL) (Sigma-L anti-sigma factor RslA)
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[rshA Rv3221A] Anti-sigma factor RshA (Regulator of SigH) (Sigma-H anti-sigma factor RshA)
[rsbW usfX Rv3287c] Anti-sigma-F factor RsbW (Anti-sigma-F factor UsfX) (Regulator of SigF) (Sigma-F anti-sigma factor RsbW)
[sigF Rv3286c] RNA polymerase sigma factor SigF (Sigma factor SigF) (Alternative RNA polymerase sigma factor SigF) (RNA polymerase sigma-F factor) (Sigma-F factor) (Stress response/stationary phase sigma factor SigF)
[rseA STM14_3233] Anti-sigma-E factor RseA (Regulator of SigE) (Sigma-E anti-sigma factor RseA) (Sigma-E factor negative regulatory protein)
[MPR1] N-acetyltransferase MPR1 (EC 2.3.1.271) ((S)-1-pyrroline-5-carboxylate acetyltransferase) (L-azetidine-2-carboxylate acetyltransferase) (AZC acetyltransferase) (Sigma1278b gene for proline-analog resistance 1)
[SIGF SIG6 SOLDAT8 At2g36990 T1J8] RNA polymerase sigma factor sigF, chloroplastic (Sigma factor F) (Sigma-F) (Protein SINGLET OXYGEN-LINKED DEATH ACTIVATOR 8) (RNA polymerase sigma factor sig6) (Atsig6) (Sigma factor 6)
[rpoE sigE b2573 JW2557] ECF RNA polymerase sigma-E factor (RNA polymerase sigma-E factor) (Sigma-24)
[sigR SCO5216] ECF RNA polymerase sigma factor SigR (ECF sigma factor SigR) (Alternative RNA polymerase sigma factor SigR) (RNA polymerase sigma-R factor) (Sigma-R factor)
[GCN4 AAS3 ARG9 YEL009C] General control protein GCN4 (Amino acid biosynthesis regulatory protein)
[FLO11 MAL5 MUC1 S1 S2 YIR019C] Flocculation protein FLO11 (Flo11p) (Flocculin-11) (Mucin-like protein 1)
[sigC Rv2069 MTCY49.08] ECF RNA polymerase sigma factor SigC (ECF sigma factor SigC) (Alternative RNA polymerase sigma factor SigC) (RNA polymerase sigma-C factor) (Sigma-C factor)
[gin Mup53] Serine recombinase gin (EC 3.1.22.-) (EC 6.5.1.-) (G-segment invertase) (Gin) (Gene product 53) (gp53)
[NPR1 YNL183C N1631] Nitrogen permease reactivator protein (EC 2.7.11.1) (Serine/threonine-protein kinase NPR1)
[rpoS appR katF nur otsX sigS b2741 JW5437] RNA polymerase sigma factor RpoS (Sigma S) (Sigma-38)
[CWP1 YKL096W YJU1 YKL443] Cell wall protein CWP1 (Glycoprotein GP40)
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[rshA MSMEG_1915 MSMEI_1875] Anti-sigma factor RshA (Regulator of SigH) (Sigma-H anti-sigma factor RshA)
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[GPB2 KRH1 YAL056W] Guanine nucleotide-binding protein subunit beta 2 (Gbeta mimic kelch protein 2)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
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[FLO1 FLO2 FLO4 FLO8 YAR050W] Flocculation protein FLO1 (Flocculin-1)
[sigL Rv0735] ECF RNA polymerase sigma factor SigL (ECF sigma factor SigL) (Alternative RNA polymerase sigma factor SigL) (RNA polymerase sigma-L factor) (Sigma-L factor)

Bibliography :
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