ID   Q1R4V1_ECOUT            Unreviewed;       212 AA.
AC   Q1R4V1;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Nucleoid occlusion factor SlmA {ECO:0000256|HAMAP-Rule:MF_01839};
GN   Name=ttk {ECO:0000313|EMBL:ABE09613.1};
GN   Synonyms=slmA {ECO:0000256|HAMAP-Rule:MF_01839};
GN   OrderedLocusNames=UTI89_C4185 {ECO:0000313|EMBL:ABE09613.1};
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106 {ECO:0000313|EMBL:ABE09613.1, ECO:0000313|Proteomes:UP000001952};
RN   [1] {ECO:0000313|EMBL:ABE09613.1, ECO:0000313|Proteomes:UP000001952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC {ECO:0000313|Proteomes:UP000001952};
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
RN   [2] {ECO:0007829|PDB:4GCL}
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
RX   PubMed=23754405; DOI=10.1073/pnas.1221036110;
RA   Tonthat N.K., Milam S.L., Chinnam N., Whitfill T., Margolin W.,
RA   Schumacher M.A.;
RT   "SlmA forms a higher-order structure on DNA that inhibits cytokinetic Z-
RT   ring formation over the nucleoid.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:10586-10591(2013).
CC   -!- FUNCTION: Required for nucleoid occlusion (NO) phenomenon, which
CC       prevents Z-ring formation and cell division over the nucleoid. Acts as
CC       a DNA-associated cell division inhibitor that binds simultaneously
CC       chromosomal DNA and FtsZ, and disrupts the assembly of FtsZ polymers.
CC       SlmA-DNA-binding sequences (SBS) are dispersed on non-Ter regions of
CC       the chromosome, preventing FtsZ polymerization at these regions.
CC       {ECO:0000256|HAMAP-Rule:MF_01839}.
CC   -!- SUBUNIT: Homodimer. Interacts with FtsZ. {ECO:0000256|HAMAP-
CC       Rule:MF_01839}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000256|HAMAP-
CC       Rule:MF_01839}.
CC   -!- SIMILARITY: Belongs to the nucleoid occlusion factor SlmA family.
CC       {ECO:0000256|HAMAP-Rule:MF_01839}.
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DR   EMBL; CP000243; ABE09613.1; -; Genomic_DNA.
DR   PDB; 4GCL; X-ray; 2.65 A; A/B/C/D/E/F/G/H=1-212.
DR   PDBsum; 4GCL; -.
DR   AlphaFoldDB; Q1R4V1; -.
DR   SMR; Q1R4V1; -.
DR   KEGG; eci:UTI89_C4185; -.
DR   HOGENOM; CLU_069356_5_0_6; -.
DR   Proteomes; UP000001952; Chromosome.
DR   GO; GO:0043590; C:bacterial nucleoid; IEA:UniProtKB-UniRule.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0010974; P:negative regulation of division septum assembly; IEA:InterPro.
DR   Gene3D; 1.10.357.10; Tetracycline Repressor, domain 2; 1.
DR   HAMAP; MF_01839; NO_factor_SlmA; 1.
DR   InterPro; IPR023772; DNA-bd_HTH_TetR-type_CS.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR001647; HTH_TetR.
DR   InterPro; IPR023769; NO_SlmA.
DR   InterPro; IPR036271; Tet_transcr_reg_TetR-rel_C_sf.
DR   PANTHER; PTHR30055; HTH-TYPE TRANSCRIPTIONAL REGULATOR RUTR; 1.
DR   PANTHER; PTHR30055:SF183; NUCLEOID OCCLUSION FACTOR SLMA; 1.
DR   Pfam; PF00440; TetR_N; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF48498; Tetracyclin repressor-like, C-terminal domain; 1.
DR   PROSITE; PS01081; HTH_TETR_1; 1.
DR   PROSITE; PS50977; HTH_TETR_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4GCL};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_01839};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_01839};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01839};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01839, ECO:0000256|PROSITE-
KW   ProRule:PRU00335}.
FT   DOMAIN          24..84
FT                   /note="HTH tetR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50977"
FT   DNA_BIND        47..66
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00335"
SQ   SEQUENCE   212 AA;  24288 MW;  378A696615488F38 CRC64;
     MPPGKCLFSG VFCNMAEKQT AKRNRREEIL QSLALMLESS DGSQRITTAK LAASVGVSEA
     ALYRHFPSKT RMFDSLIEFI EDSLITRINL ILKDEKDTTA RLRLIVLLLL GFGERNPGLT
     RILTGHALMF EQDRLQGRIN QLFERIEAQL RQVLREKRMR EGEGYATDET LLASQILAFC
     EGMLSRFVRS EFKYRPTDDF DARWPLIAAQ LQ
//