ID   SULA_SALPK              Reviewed;         169 AA.
AC   B5BBK9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, 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=SSPA1652;
OS   Salmonella paratyphi A (strain AKU_12601).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=554290;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AKU_12601;
RX   PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA   Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA   Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA   Mungall K., Dougan G., Parkhill J.;
RT   "Pseudogene accumulation in the evolutionary histories of Salmonella
RT   enterica serovars Paratyphi A and Typhi.";
RL   BMC Genomics 10:36-36(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; FM200053; CAR59844.1; -; Genomic_DNA.
DR   RefSeq; WP_000288732.1; NC_011147.1.
DR   AlphaFoldDB; B5BBK9; -.
DR   SMR; B5BBK9; -.
DR   KEGG; sek:SSPA1652; -.
DR   HOGENOM; CLU_118972_1_0_6; -.
DR   OMA; YGFIMRP; -.
DR   Proteomes; UP000001869; 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_1000138170"
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;  19013 MW;  3848A73595E5D176 CRC64;
     MYTSGYANRS SSFPTTTHNA ARTATENAAA GLVSEVVYHE DQPMMAQLLL LPLLRQLGQQ
     SRWQLWLTPQ QKLSREWVQS SGLPLTKVMQ ISQLAPRHTL ESMIRALRTG NYSVVIGWMT
     EELTEEEHAS LVEAAKVGNA VGFIMRPVRA HALPRRQHSG LKIHSNLYH