SULA_ECO8A
ID SULA_ECO8A Reviewed; 169 AA.
AC B7M887;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Cell division inhibitor SulA {ECO:0000255|HAMAP-Rule:MF_01179};
GN Name=sulA {ECO:0000255|HAMAP-Rule:MF_01179}; OrderedLocusNames=ECIAI1_0999;
OS Escherichia coli O8 (strain IAI1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585034;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI1;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(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; CU928160; CAQ97863.1; -; Genomic_DNA.
DR RefSeq; WP_000288710.1; NC_011741.1.
DR AlphaFoldDB; B7M887; -.
DR SMR; B7M887; -.
DR GeneID; 66670766; -.
DR KEGG; ecr:ECIAI1_0999; -.
DR HOGENOM; CLU_118972_1_0_6; -.
DR OMA; YGFIMRP; -.
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_1000138158"
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; 18801 MW; C76B4493773C77C2 CRC64;
MYTSGYAHRS SSFSSAASKI ARVSTENTTA GLISEVVYRE DQPMMTQLLL LPLLQQLGQQ
SRWQLWLTPQ QKLSREWVQA SGLPLTKVMQ ISQLSPCHTV ESMVRALRTG NYSVVIGWLA
DDLTEEEHAE LVDAANEGNA MGFIMRPVSA SSHATRQLSG LKIHSNLYH
