SULA_PHOLL
ID SULA_PHOLL Reviewed; 177 AA.
AC Q7N601;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cell division inhibitor SulA {ECO:0000255|HAMAP-Rule:MF_01179};
GN Name=sulA {ECO:0000255|HAMAP-Rule:MF_01179}; OrderedLocusNames=plu1776;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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; BX571865; CAE14069.1; -; Genomic_DNA.
DR RefSeq; WP_011146054.1; NC_005126.1.
DR AlphaFoldDB; Q7N601; -.
DR SMR; Q7N601; -.
DR STRING; 243265.plu1776; -.
DR PRIDE; Q7N601; -.
DR EnsemblBacteria; CAE14069; CAE14069; plu1776.
DR GeneID; 24166857; -.
DR KEGG; plu:plu1776; -.
DR eggNOG; COG5404; Bacteria.
DR HOGENOM; CLU_118972_0_0_6; -.
DR OMA; YGFIMRP; -.
DR OrthoDB; 1941503at2; -.
DR BioCyc; PLUM243265:PLU_RS08900-MON; -.
DR Proteomes; UP000002514; 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; Reference proteome; Septation;
KW SOS response.
FT CHAIN 1..177
FT /note="Cell division inhibitor SulA"
FT /id="PRO_0000343968"
FT REGION 112..118
FT /note="FtsZ binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01179"
FT REGION 170..177
FT /note="Lon protease binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01179"
FT SITE 177
FT /note="Essential for degradation by Lon protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01179"
SQ SEQUENCE 177 AA; 19940 MW; BCB37DD027720FE6 CRC64;
MGIQSSWFYS SKHQSAKREG MVKEGKGGIV SELIYSNNQY SDNQYSDNQA VINRILLPLL
RQSGNEARWL LWVSPHKKLS RQWLINSGLP LDKIIQLNRM SSITTVEAME RALASGNYSV
VLGWLPTLSG KDTVRLQAAA QKGNALGFIM RPQDVSKETS RAESRSDLLK IHSIHYH
