ID   SULA_SALPC              Reviewed;         169 AA.
AC   C0Q8D4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Cell division inhibitor SulA {ECO:0000255|HAMAP-Rule:MF_01179};
GN   Name=sulA {ECO:0000255|HAMAP-Rule:MF_01179}; OrderedLocusNames=SPC_2678;
OS   Salmonella paratyphi C (strain RKS4594).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=476213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKS4594;
RX   PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA   Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA   Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT   "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT   and pathogenic convergence with Salmonella typhi.";
RL   PLoS ONE 4:E4510-E4510(2009).
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; CP000857; ACN46779.1; -; Genomic_DNA.
DR   RefSeq; WP_000288731.1; NC_012125.1.
DR   AlphaFoldDB; C0Q8D4; -.
DR   SMR; C0Q8D4; -.
DR   EnsemblBacteria; ACN46779; ACN46779; SPC_2678.
DR   KEGG; sei:SPC_2678; -.
DR   HOGENOM; CLU_118972_1_0_6; -.
DR   OMA; YGFIMRP; -.
DR   Proteomes; UP000001599; 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_1000164431"
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;  18994 MW;  99F2A73595E5D166 CRC64;
     MYTSGYANRS SSFPTTTHNA ARTATENAAA GLVSEVVYHE DQPMMAQLLL LPLLRQLGQQ
     SRWQLWLTPQ QKLSREWVQS SGLPLTKVMQ ISQLAPRHTL ESMIRALRTG NYSVVIGWMT
     EELTEEEHAS LVEAAKVGNA VGFIMHPVRA HALPRRQHSG LKIHSNLYH