SULA_SALEP
ID SULA_SALEP Reviewed; 169 AA.
AC B5QZG1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Cell division inhibitor SulA {ECO:0000255|HAMAP-Rule:MF_01179};
GN Name=sulA {ECO:0000255|HAMAP-Rule:MF_01179}; OrderedLocusNames=SEN0936;
OS Salmonella enteritidis PT4 (strain P125109).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P125109;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
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; AM933172; CAR32519.1; -; Genomic_DNA.
DR RefSeq; WP_000288733.1; NC_011294.1.
DR AlphaFoldDB; B5QZG1; -.
DR SMR; B5QZG1; -.
DR KEGG; set:SEN0936; -.
DR HOGENOM; CLU_118972_1_0_6; -.
DR OMA; YGFIMRP; -.
DR Proteomes; UP000000613; 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_1000138166"
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; 19003 MW; 85D8A73595E5D175 CRC64;
MYTSGYANRS SSFPTTTHNA ARTATENAAA GLVSEVVYHE DQPMMAQLLL LPLLRQLGQQ
SRWQLWLTPQ QKLSREWVQS SGLPLTKVMQ ISQLAPRHTL ESMIRALRTG NYSVVIGWMT
EELTEEEHAS LVEAAKVGNA VGFIMRPVRA HALSRRQHSG LKIHSNLYH