SULA_CROTZ
ID SULA_CROTZ Reviewed; 168 AA.
AC C9Y0Q0;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Cell division inhibitor SulA {ECO:0000255|HAMAP-Rule:MF_01179};
GN Name=sulA {ECO:0000255|HAMAP-Rule:MF_01179}; OrderedLocusNames=Ctu_15660;
OS Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=693216;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032;
RX PubMed=21037008; DOI=10.1128/jb.01162-10;
RA Stephan R., Lehner A., Tischler P., Rattei T.;
RT "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT pathogen causing deaths in neonates.";
RL J. Bacteriol. 193:309-310(2011).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBA29741.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FN543093; CBA29741.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041923404.1; NC_013282.2.
DR AlphaFoldDB; C9Y0Q0; -.
DR SMR; C9Y0Q0; -.
DR EnsemblBacteria; CBA29741; CBA29741; CTU_15660.
DR GeneID; 60373858; -.
DR KEGG; ctu:CTU_15660; -.
DR PATRIC; fig|693216.3.peg.1493; -.
DR HOGENOM; CLU_118972_2_0_6; -.
DR Proteomes; UP000002069; 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.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; DNA damage; Septation; SOS response.
FT CHAIN 1..168
FT /note="Cell division inhibitor SulA"
FT /id="PRO_0000414243"
FT REGION 105..111
FT /note="FtsZ binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01179"
FT REGION 161..168
FT /note="Lon protease binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01179"
FT SITE 168
FT /note="Essential for degradation by Lon protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01179"
SQ SEQUENCE 168 AA; 19270 MW; 62F5DFC1575A551F CRC64;
MYFSHQNRAH GSRRLAKETA DALAQAETRG LISEVMYNED QPRMTQMVLL PLLQQLGLQS
RWQLWLTPQQ RLSREWVESA GLPLTKVMQV SQMNPQVTLD SMIRALETGN YSVVIAWLHD
DLTDDEHRRL TEAAEKGNAM GFLMRPVQPS LPGDRPRSGL RIHSRMVH
