SULA_ECOLI
ID SULA_ECOLI Reviewed; 169 AA.
AC P0AFZ5; P03840; P08846; P71224;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Cell division inhibitor SulA;
GN Name=sulA; Synonyms=sfiA; OrderedLocusNames=b0958, JW0941;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6253901; DOI=10.1093/nar/8.13.3011;
RA Beck E., Bremer E.;
RT "Nucleotide sequence of the gene ompA coding the outer membrane protein II
RT of Escherichia coli K-12.";
RL Nucleic Acids Res. 8:3011-3027(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX PubMed=3297925; DOI=10.1016/0378-1119(87)90392-1;
RA Freudl R., Braun G., Honore N., Cole S.T.;
RT "Evolution of the enterobacterial sulA gene: a component of the SOS system
RT encoding an inhibitor of cell division.";
RL Gene 52:31-40(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RX PubMed=6306396; DOI=10.1007/bf00325901;
RA Cole S.T.;
RT "Characterisation of the promoter for the LexA regulated sulA gene of
RT Escherichia coli.";
RL Mol. Gen. Genet. 189:400-404(1983).
RN [7]
RP DEGRADATION BY LON PROTEASE.
RC STRAIN=K12 / C600 / CR34 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
RX PubMed=6300834; DOI=10.1073/pnas.80.2.358;
RA Mizusawa S., Gottesman S.;
RT "Protein degradation in Escherichia coli: the lon gene controls the
RT stability of sulA protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:358-362(1983).
RN [8]
RP ROLE IN BLOCKING SEPTATION.
RC STRAIN=K12;
RX PubMed=6087326; DOI=10.1073/pnas.81.14.4490;
RA Huisman O., D'Ari R., Gottesman S.;
RT "Cell-division control in Escherichia coli: specific induction of the SOS
RT function SfiA protein is sufficient to block septation.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4490-4494(1984).
RN [9]
RP INTERACTION WITH FTSZ.
RC STRAIN=K12;
RX PubMed=2994059; DOI=10.1073/pnas.82.18.6045;
RA Jones C., Holland I.B.;
RT "Role of the SulB (FtsZ) protein in division inhibition during the SOS
RT response in Escherichia coli: FtsZ stabilizes the inhibitor SulA in
RT maxicells.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:6045-6049(1985).
RN [10]
RP ROLE IN THE INHIBITION OF Z-RING FORMATION.
RC STRAIN=K12;
RX PubMed=2145263; DOI=10.1128/jb.172.10.5602-5609.1990;
RA Bi E., Lutkenhaus J.;
RT "Analysis of ftsZ mutations that confer resistance to the cell division
RT inhibitor SulA (SfiA).";
RL J. Bacteriol. 172:5602-5609(1990).
RN [11]
RP ROLE IN THE INHIBITION OF Z-RING FORMATION.
RC STRAIN=K12;
RX PubMed=8432706; DOI=10.1128/jb.175.4.1118-1125.1993;
RA Bi E., Lutkenhaus J.;
RT "Cell division inhibitors SulA and MinCD prevent formation of the FtsZ
RT ring.";
RL J. Bacteriol. 175:1118-1125(1993).
RN [12]
RP INTERACTION WITH FTSZ.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7726836; DOI=10.1006/bbrc.1995.1489;
RA Higashitani A., Higashitani N., Horiuchi K.;
RT "A cell division inhibitor SulA of Escherichia coli directly interacts with
RT FtsZ through GTP hydrolysis.";
RL Biochem. Biophys. Res. Commun. 209:198-204(1995).
RN [13]
RP MUTAGENESIS OF ARG-62 AND LEU-83.
RX PubMed=8752322; DOI=10.1128/jb.178.17.5080-5085.1996;
RA Huang J., Cao C., Lutkenhaus J.;
RT "Interaction between FtsZ and inhibitors of cell division.";
RL J. Bacteriol. 178:5080-5085(1996).
RN [14]
RP MUTAGENESIS OF ARG-39; ARG-62; LEU-67; LYS-72; ARG-75; GLU-76; TRP-77;
RP LYS-87; HIS-98; ARG-105; ARG-108; VAL-115; GLY-117; GLU-126 AND HIS-128.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9180687; DOI=10.1007/s004380050426;
RA Higashitani A., Ishii Y., Kato Y., Koriuchi K.;
RT "Functional dissection of a cell-division inhibitor, SulA, of Escherichia
RT coli and its negative regulation by Lon.";
RL Mol. Gen. Genet. 254:351-357(1997).
RN [15]
RP FUNCTION.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=9501185; DOI=10.1073/pnas.95.6.2885;
RA Mukherjee A., Cao C., Lutkenhaus J.;
RT "Inhibition of FtsZ polymerization by SulA, an inhibitor of septation in
RT Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:2885-2890(1998).
RN [16]
RP INHIBITION OF FTSZ POLYMERIZATION.
RX PubMed=9683493; DOI=10.1128/jb.180.15.3946-3953.1998;
RA Trusca D., Scott S., Thompson C., Bramhill D.;
RT "Bacterial SOS checkpoint protein SulA inhibits polymerization of purified
RT FtsZ cell division protein.";
RL J. Bacteriol. 180:3946-3953(1998).
RN [17]
RP DEGRADATION BY LON PROTEASE, LON BINDING SITE, AND MUTAGENESIS OF ILE-163;
RP HIS-164; LEU-167 AND HIS-169.
RC STRAIN=K12;
RX PubMed=10788793; DOI=10.1093/oxfordjournals.jbchem.a022677;
RA Ishii Y., Sonezaki S., Iwasaki Y., Miyata Y., Akita K., Kato Y., Amano F.;
RT "Regulatory role of C-terminal residues of SulA in its degradation by Lon
RT protease in Escherichia coli.";
RL J. Biochem. 127:837-844(2000).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10931335; DOI=10.1046/j.1365-2958.2000.02007.x;
RA Justice S.S., Garcia-Lara J., Rothfield L.I.;
RT "Cell division inhibitors SulA and MinC/MinD block septum formation at
RT different steps in the assembly of the Escherichia coli division
RT machinery.";
RL Mol. Microbiol. 37:410-423(2000).
RN [19]
RP ROLE OF HIS-169 IN DEGRADATION BY LON PROTEASE.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=11513747; DOI=10.1042/0264-6021:3580473;
RA Ishii Y., Amano F.;
RT "Regulation of SulA cleavage by Lon protease by the C-terminal amino acid
RT of SulA, histidine.";
RL Biochem. J. 358:473-480(2001).
RN [20]
RP FUNCTION IN REGULATION OF FTSZ ASSEMBLY.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=18245292; DOI=10.1128/jb.01612-07;
RA Dajkovic A., Mukherjee A., Lutkenhaus J.;
RT "Investigation of regulation of FtsZ assembly by SulA and development of a
RT model for FtsZ polymerization.";
RL J. Bacteriol. 190:2513-2526(2008).
RN [21]
RP INDUCTION BY HYDROXYUREA.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [22]
RP NEUTRALIZED BY CBEA.
RC STRAIN=K12 / BW25113;
RX PubMed=22515815; DOI=10.1111/j.1365-2958.2012.08068.x;
RA Masuda H., Tan Q., Awano N., Wu K.P., Inouye M.;
RT "YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ,
RT antagonizing the CbtA (YeeV) toxicity in Escherichia coli.";
RL Mol. Microbiol. 84:979-989(2012).
CC -!- FUNCTION: Component of the SOS system and an inhibitor of cell
CC division. Accumulation of SulA causes rapid cessation of cell division
CC and the appearance of long, non-septate filaments. In the presence of
CC GTP, binds a polymerization-competent form of FtsZ in a 1:1 ratio, thus
CC inhibiting FtsZ polymerization and therefore preventing it from
CC participating in the assembly of the Z ring. This mechanism prevents
CC the premature segregation of damaged DNA to daughter cells during cell
CC division. The effect of overexpression of SulA is neutralized by
CC antitoxin CbeA (yeeU) (PubMed:22515815). {ECO:0000269|PubMed:10931335,
CC ECO:0000269|PubMed:18245292, ECO:0000269|PubMed:2145263,
CC ECO:0000269|PubMed:22515815, ECO:0000269|PubMed:6087326,
CC ECO:0000269|PubMed:8432706, ECO:0000269|PubMed:9501185}.
CC -!- SUBUNIT: Interacts with FtsZ. {ECO:0000269|PubMed:2994059,
CC ECO:0000269|PubMed:7726836}.
CC -!- INTERACTION:
CC P0AFZ5; P0A6H5: hslU; NbExp=5; IntAct=EBI-2012039, EBI-369317;
CC -!- INDUCTION: By DNA damage, as part of the SOS response, repressed by
CC LexA (PubMed:3297925). Induced 8-fold by hydroxyurea (at protein level)
CC (PubMed:20005847). {ECO:0000269|PubMed:20005847,
CC ECO:0000269|PubMed:3297925}.
CC -!- PTM: Is rapidly cleaved and degraded by the Lon protease once DNA
CC damage is repaired. {ECO:0000269|PubMed:10788793,
CC ECO:0000269|PubMed:11513747, ECO:0000269|PubMed:6300834,
CC ECO:0000269|PubMed:9180687}.
CC -!- SIMILARITY: Belongs to the SulA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA23587.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; V00307; CAA23587.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC74044.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35716.1; -; Genomic_DNA.
DR EMBL; V00358; CAA23654.1; -; Genomic_DNA.
DR PIR; A29016; QQECA1.
DR RefSeq; NP_415478.1; NC_000913.3.
DR RefSeq; WP_000288710.1; NZ_STEB01000006.1.
DR AlphaFoldDB; P0AFZ5; -.
DR SMR; P0AFZ5; -.
DR BioGRID; 4259653; 213.
DR DIP; DIP-10945N; -.
DR IntAct; P0AFZ5; 2.
DR STRING; 511145.b0958; -.
DR ChEMBL; CHEMBL1287594; -.
DR PaxDb; P0AFZ5; -.
DR PRIDE; P0AFZ5; -.
DR EnsemblBacteria; AAC74044; AAC74044; b0958.
DR EnsemblBacteria; BAA35716; BAA35716; BAA35716.
DR GeneID; 66670766; -.
DR GeneID; 947335; -.
DR KEGG; ecj:JW0941; -.
DR KEGG; eco:b0958; -.
DR PATRIC; fig|1411691.4.peg.1316; -.
DR EchoBASE; EB0977; -.
DR eggNOG; COG5404; Bacteria.
DR HOGENOM; CLU_118972_1_0_6; -.
DR OMA; YGFIMRP; -.
DR PhylomeDB; P0AFZ5; -.
DR BioCyc; EcoCyc:EG10984-MON; -.
DR PRO; PR:P0AFZ5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0051782; P:negative regulation of cell division; IMP:EcoliWiki.
DR GO; GO:0032466; P:negative regulation of cytokinesis; IMP:EcoliWiki.
DR GO; GO:2000245; P:negative regulation of FtsZ-dependent cytokinesis; IMP:EcoCyc.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IDA:EcoCyc.
DR GO; GO:0032272; P:negative regulation of protein polymerization; IDA:EcoCyc.
DR GO; GO:0009432; P:SOS response; IEP:EcoCyc.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01179; SulA; 1.
DR InterPro; IPR004596; Cell_div_suppressor_SulA.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF03846; SulA; 1.
DR PIRSF; PIRSF003093; SulA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00623; sula; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; DNA damage; Reference proteome; Septation;
KW SOS response.
FT CHAIN 1..169
FT /note="Cell division inhibitor SulA"
FT /id="PRO_0000072305"
FT REGION 106..112
FT /note="FtsZ binding"
FT /evidence="ECO:0000250"
FT REGION 162..169
FT /note="Lon protease binding"
FT SITE 169
FT /note="Essential for degradation by Lon protease"
FT MUTAGEN 39
FT /note="R->A: No effect on degradation by Lon protease."
FT /evidence="ECO:0000269|PubMed:9180687"
FT MUTAGEN 62
FT /note="R->A: Loss of degradation by Lon protease."
FT /evidence="ECO:0000269|PubMed:8752322,
FT ECO:0000269|PubMed:9180687"
FT MUTAGEN 62
FT /note="R->C,H,S: Loss of activity due to loss of ability to
FT bind to FtsZ."
FT /evidence="ECO:0000269|PubMed:8752322,
FT ECO:0000269|PubMed:9180687"
FT MUTAGEN 67
FT /note="L->A: Loss of degradation by Lon protease."
FT /evidence="ECO:0000269|PubMed:9180687"
FT MUTAGEN 72
FT /note="K->A: No effect on degradation by Lon protease."
FT /evidence="ECO:0000269|PubMed:9180687"
FT MUTAGEN 75
FT /note="R->A: No effect on degradation by Lon protease."
FT /evidence="ECO:0000269|PubMed:9180687"
FT MUTAGEN 76
FT /note="E->A: No effect on degradation by Lon protease."
FT /evidence="ECO:0000269|PubMed:9180687"
FT MUTAGEN 77
FT /note="W->A: Loss of degradation by Lon protease."
FT /evidence="ECO:0000269|PubMed:9180687"
FT MUTAGEN 83
FT /note="L->R: Loss of activity due to loss of ability to
FT bind to FtsZ."
FT /evidence="ECO:0000269|PubMed:8752322"
FT MUTAGEN 87
FT /note="K->A: Loss of degradation by Lon protease."
FT /evidence="ECO:0000269|PubMed:9180687"
FT MUTAGEN 98
FT /note="H->A: No effect on degradation by Lon protease."
FT /evidence="ECO:0000269|PubMed:9180687"
FT MUTAGEN 105
FT /note="R->A: No effect on degradation by Lon protease."
FT /evidence="ECO:0000269|PubMed:9180687"
FT MUTAGEN 108
FT /note="R->A: No effect on degradation by Lon protease."
FT /evidence="ECO:0000269|PubMed:9180687"
FT MUTAGEN 115
FT /note="V->A: No effect on degradation by Lon protease."
FT /evidence="ECO:0000269|PubMed:9180687"
FT MUTAGEN 117
FT /note="G->A: No effect on degradation by Lon protease."
FT /evidence="ECO:0000269|PubMed:9180687"
FT MUTAGEN 126
FT /note="E->A: No effect on degradation by Lon protease."
FT /evidence="ECO:0000269|PubMed:9180687"
FT MUTAGEN 128
FT /note="H->A: No effect on degradation by Lon protease."
FT /evidence="ECO:0000269|PubMed:9180687"
FT MUTAGEN 163
FT /note="I->A: Slight decrease in degradation by Lon
FT protease."
FT /evidence="ECO:0000269|PubMed:10788793"
FT MUTAGEN 164
FT /note="H->A: No effect on degradation by Lon protease."
FT /evidence="ECO:0000269|PubMed:10788793"
FT MUTAGEN 167
FT /note="L->A: Slight decrease in degradation by Lon
FT protease."
FT /evidence="ECO:0000269|PubMed:10788793"
FT MUTAGEN 169
FT /note="H->A: Great decrease in degradation by Lon
FT protease."
FT /evidence="ECO:0000269|PubMed:10788793"
SQ SEQUENCE 169 AA; 18801 MW; C76B4493773C77C2 CRC64;
MYTSGYAHRS SSFSSAASKI ARVSTENTTA GLISEVVYRE DQPMMTQLLL LPLLQQLGQQ
SRWQLWLTPQ QKLSREWVQA SGLPLTKVMQ ISQLSPCHTV ESMVRALRTG NYSVVIGWLA
DDLTEEEHAE LVDAANEGNA MGFIMRPVSA SSHATRQLSG LKIHSNLYH
