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SULA_SALTY
ID   SULA_SALTY              Reviewed;         169 AA.
AC   P0A241; P08847;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Cell division inhibitor SulA {ECO:0000255|HAMAP-Rule:MF_01179};
GN   Name=sulA {ECO:0000255|HAMAP-Rule:MF_01179}; OrderedLocusNames=STM1071;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3297925; DOI=10.1016/0378-1119(87)90392-1;
RA   Freudl R., Braun G., Honore N., Cole S.T.;
RT   "Evolution of the enterobacterial sulA gene: a component of the SOS system
RT   encoding an inhibitor of cell division.";
RL   Gene 52:31-40(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; M16324; AAA27230.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20004.1; -; Genomic_DNA.
DR   PIR; B29016; B29016.
DR   RefSeq; NP_460045.1; NC_003197.2.
DR   RefSeq; WP_000288732.1; NC_003197.2.
DR   AlphaFoldDB; P0A241; -.
DR   SMR; P0A241; -.
DR   STRING; 99287.STM1071; -.
DR   PaxDb; P0A241; -.
DR   EnsemblBacteria; AAL20004; AAL20004; STM1071.
DR   GeneID; 1252589; -.
DR   KEGG; stm:STM1071; -.
DR   PATRIC; fig|99287.12.peg.1136; -.
DR   HOGENOM; CLU_118972_1_0_6; -.
DR   OMA; YGFIMRP; -.
DR   PhylomeDB; P0A241; -.
DR   BioCyc; SENT99287:STM1071-MON; -.
DR   Proteomes; UP000001014; 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; IBA:GO_Central.
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_0000072309"
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"
FT   CONFLICT        102
FT                   /note="S -> T (in Ref. 1; AAA27230)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108
FT                   /note="R -> A (in Ref. 1; AAA27230)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        151
FT                   /note="H -> L (in Ref. 1; AAA27230)"
FT                   /evidence="ECO:0000305"
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
 
 
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