ID A0A068R8I0_9GAMM Unreviewed; 199 AA.
AC A0A068R8I0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Nucleoid occlusion factor SlmA {ECO:0000256|HAMAP-Rule:MF_01839};
GN Name=slmA {ECO:0000256|HAMAP-Rule:MF_01839,
GN ECO:0000313|EMBL:CDG23279.1};
GN ORFNames=XPG1_3652 {ECO:0000313|EMBL:CDG23279.1};
OS Xenorhabdus poinarii G6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1354304 {ECO:0000313|EMBL:CDG23279.1, ECO:0000313|Proteomes:UP000032735};
RN [1] {ECO:0000313|EMBL:CDG23279.1, ECO:0000313|Proteomes:UP000032735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G6 {ECO:0000313|EMBL:CDG23279.1,
RC ECO:0000313|Proteomes:UP000032735};
RA Genoscope - CEA;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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; FO704551; CDG23279.1; -; Genomic_DNA.
DR RefSeq; WP_045960230.1; NZ_FO704551.1.
DR AlphaFoldDB; A0A068R8I0; -.
DR STRING; 1354304.XPG1_3652; -.
DR KEGG; xpo:XPG1_3652; -.
DR HOGENOM; CLU_069356_5_0_6; -.
DR OrthoDB; 9179041at2; -.
DR Proteomes; UP000032735; 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 3: Inferred from homology;
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 10..71
FT /note="HTH tetR-type"
FT /evidence="ECO:0000259|PROSITE:PS50977"
FT DNA_BIND 34..53
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00335"
SQ SEQUENCE 199 AA; 23303 MW; 02947C89CAEECD32 CRC64;
MAEKERTKKK NRREEILQAL AHMLESSDGS QRITTAKLAA NVGVSEAALY RHFPSKTRMF
DSLIEFIEDS LISRINLILQ DEKDTITRIR LILALLLGFA EKNPGLTRIM TGHALMFEQD
RLQNRINQLF ERIEMQLRQI LKEKKIRDGQ GFNYDETVLA SQLLAFCEGM LSRFVRSEFR
YRPTTEFEVR WPLILIQLK
//