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SULA_SHIFL
ID   SULA_SHIFL              Reviewed;         169 AA.
AC   Q83RX1; Q7UD16;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 4.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Cell division inhibitor SulA {ECO:0000255|HAMAP-Rule:MF_01179};
GN   Name=sulA {ECO:0000255|HAMAP-Rule:MF_01179};
GN   OrderedLocusNames=SF0958, S1024;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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. {ECO:0000255|HAMAP-Rule:MF_01179}.
CC   -!- SUBUNIT: Interacts with FtsZ. {ECO:0000255|HAMAP-Rule:MF_01179}.
CC   -!- INDUCTION: By DNA damage, as part of the SOS response.
CC       {ECO:0000255|HAMAP-Rule:MF_01179}.
CC   -!- PTM: Is rapidly cleaved and degraded by the Lon protease once DNA
CC       damage is repaired. {ECO:0000255|HAMAP-Rule:MF_01179}.
CC   -!- SIMILARITY: Belongs to the SulA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01179}.
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DR   EMBL; AE005674; AAN42587.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16472.1; -; Genomic_DNA.
DR   RefSeq; NP_706880.2; NC_004337.2.
DR   RefSeq; WP_000288715.1; NZ_WPGW01000054.1.
DR   AlphaFoldDB; Q83RX1; -.
DR   SMR; Q83RX1; -.
DR   STRING; 198214.SF0958; -.
DR   EnsemblBacteria; AAN42587; AAN42587; SF0958.
DR   EnsemblBacteria; AAP16472; AAP16472; S1024.
DR   GeneID; 1023924; -.
DR   KEGG; sfl:SF0958; -.
DR   KEGG; sfx:S1024; -.
DR   PATRIC; fig|198214.7.peg.1116; -.
DR   HOGENOM; CLU_118972_1_0_6; -.
DR   OMA; YGFIMRP; -.
DR   OrthoDB; 1941503at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0051782; P:negative regulation of cell division; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
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_0000343976"
FT   REGION          106..112
FT                   /note="FtsZ binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01179"
FT   REGION          162..169
FT                   /note="Lon protease binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01179"
FT   SITE            169
FT                   /note="Essential for degradation by Lon protease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01179"
SQ   SEQUENCE   169 AA;  18861 MW;  C6C1F4936D8C77D2 CRC64;
     MYTSGYAHRS SSFSSAASKI ARVSTENTTA GLISEVVYRE DQPMMTQLLL LPLLQQLGQQ
     SRWQLWLTPQ QKLSREWVQA SGLPLTKVMQ ISQLSPCHTV ESMVRALRTG NYSVVIGWLT
     DDLTEEEHAE LVDAANEGNA MGFIMRPVSA SSHTTRQLSG LKIHSNLYH
 
 
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