SULA_YERPS
ID SULA_YERPS Reviewed; 168 AA.
AC Q66CE9;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Cell division inhibitor SulA {ECO:0000255|HAMAP-Rule:MF_01179};
GN Name=sulA {ECO:0000255|HAMAP-Rule:MF_01179}; OrderedLocusNames=YPTB1454;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH20694.1; -; Genomic_DNA.
DR RefSeq; WP_011192069.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66CE9; -.
DR SMR; Q66CE9; -.
DR EnsemblBacteria; CAH20694; CAH20694; YPTB1454.
DR GeneID; 66842111; -.
DR KEGG; ypo:BZ17_1064; -.
DR KEGG; yps:YPTB1454; -.
DR PATRIC; fig|273123.14.peg.1129; -.
DR OMA; YGFIMRP; -.
DR Proteomes; UP000001011; 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_0000343984"
FT REGION 106..112
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; 19030 MW; 560EDCDE200E92F2 CRC64;
MRTQSLKPYH ANYHSLTTND SPARVDAPTD SGLISEFVYS ENQPVVTQLL LPLLQQLSKQ
SRWLLWLTPQ QKLSRSWLKQ SGLPINKVVQ LRQINPLSTV EAMEKALLTG NYSVVLGWLP
ELTEDDRIRL RLAAKLGNAY GFVMRPLNDT KVGSGQCATL KIHSYLYH
