ID   SULA_SERP5              Reviewed;         168 AA.
AC   A8GCL9;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Cell division inhibitor SulA {ECO:0000255|HAMAP-Rule:MF_01179};
GN   Name=sulA {ECO:0000255|HAMAP-Rule:MF_01179}; OrderedLocusNames=Spro_1755;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000826; ABV40859.1; -; Genomic_DNA.
DR   RefSeq; WP_012006182.1; NC_009832.1.
DR   AlphaFoldDB; A8GCL9; -.
DR   SMR; A8GCL9; -.
DR   STRING; 399741.Spro_1755; -.
DR   EnsemblBacteria; ABV40859; ABV40859; Spro_1755.
DR   KEGG; spe:Spro_1755; -.
DR   eggNOG; COG5404; Bacteria.
DR   HOGENOM; CLU_118972_1_0_6; -.
DR   OMA; YGFIMRP; -.
DR   OrthoDB; 1941503at2; -.
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..168
FT                   /note="Cell division inhibitor SulA"
FT                   /id="PRO_0000343974"
FT   REGION          106..112
FT                   /note="FtsZ binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01179"
FT   REGION          161..168
FT                   /note="Lon protease binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01179"
FT   SITE            168
FT                   /note="Essential for degradation by Lon protease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01179"
SQ   SEQUENCE   168 AA;  18960 MW;  7C0F131800F05399 CRC64;
     MRTQSLYNTH FSHTSFAVSN AAESTNDGKE NGLISELVYN EHQPAVVQLL LPLLQQLGMQ
     SRWLLWLTPQ QKLSKLWLQQ SGLPVGKVVQ LSQINSLDTV EAMEKALLTG NYSVVLGWLP
     DLTEEDRLKL RRAAELGNAY GFIMRPQRDI NPVHGHCSTL KIHSSLYH