ID   SULA_ERWP6              Reviewed;         168 AA.
AC   D2TDA7;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 2.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Cell division inhibitor SulA {ECO:0000255|HAMAP-Rule:MF_01179};
GN   Name=sulA {ECO:0000255|HAMAP-Rule:MF_01179}; OrderedLocusNames=EPYR_02411;
OS   Erwinia pyrifoliae (strain DSM 12163 / CIP 106111 / Ep16/96).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=644651;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12163 / CIP 106111 / Ep16/96;
RX   PubMed=20047678; DOI=10.1186/1471-2164-11-2;
RA   Smits T.H., Jaenicke S., Rezzonico F., Kamber T., Goesmann A., Frey J.E.,
RA   Duffy B.;
RT   "Complete genome sequence of the fire blight pathogen Erwinia pyrifoliae
RT   DSM 12163T and comparative genomic insights into plant pathogenicity.";
RL   BMC Genomics 11:2-2(2010).
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=CAY74791.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; FN392235; CAY74791.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_012668519.1; NC_017390.1.
DR   AlphaFoldDB; D2TDA7; -.
DR   SMR; D2TDA7; -.
DR   EnsemblBacteria; CAY74791; CAY74791; EPYR_02411.
DR   KEGG; epr:EPYR_02411; -.
DR   PATRIC; fig|644651.3.peg.2200; -.
DR   HOGENOM; CLU_118972_2_0_6; -.
DR   Proteomes; UP000008690; 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_0000414246"
FT   REGION          105..111
FT                   /note="FtsZ 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;  18853 MW;  6EB5764FC2FFEB14 CRC64;
     MRTHFMKNQS VKRNQHVSTP AIPASICADG LISELVHNED HPGMTQLLLL PLLQQLGTQS
     RWQLWLTSQQ KLSRDWLLRS GLPLDKVMQS PYCGTITTVE AMIKALQTGN YSVVLGWLAD
     EISETERKRL QQAAKSGQAL GLIMRSECNV LPSARPLHGL RIQSSLYH