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SULA_ENT38
ID   SULA_ENT38              Reviewed;         169 AA.
AC   A4W8X0;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Cell division inhibitor SulA {ECO:0000255|HAMAP-Rule:MF_01179};
GN   Name=sulA {ECO:0000255|HAMAP-Rule:MF_01179}; OrderedLocusNames=Ent638_1470;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(2010).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABP60150.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000653; ABP60150.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041689358.1; NC_009436.1.
DR   AlphaFoldDB; A4W8X0; -.
DR   SMR; A4W8X0; -.
DR   STRING; 399742.Ent638_1470; -.
DR   EnsemblBacteria; ABP60150; ABP60150; Ent638_1470.
DR   KEGG; ent:Ent638_1470; -.
DR   eggNOG; COG5404; Bacteria.
DR   HOGENOM; CLU_118972_1_0_6; -.
DR   OrthoDB; 1941503at2; -.
DR   Proteomes; UP000000230; 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; Septation; SOS response.
FT   CHAIN           1..169
FT                   /note="Cell division inhibitor SulA"
FT                   /id="PRO_0000343956"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  18940 MW;  D54059D21BFCE609 CRC64;
     MHTSIYANRS TSFSPSAGND TQNTFGRVST GMISEVVYRE DQPLMTQLLL LPLLQQLGQQ
     SRWQLWLTPK QKLSREWVQS AGLPLAKVMQ ISQIAPCHTV DSMIRALRTG NYSVVIGWLS
     EELTEDEHFR LVEAAEEGNA IGLIMRPVNP DSLGRGHLSG LKIHSNLYH
 
 
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