ID I3DC09_HAEPH Unreviewed; 202 AA.
AC I3DC09;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Nucleoid occlusion factor SlmA {ECO:0000256|HAMAP-Rule:MF_01839};
GN Name=slmA {ECO:0000256|HAMAP-Rule:MF_01839};
GN ORFNames=HMPREF1050_0971 {ECO:0000313|EMBL:EIJ69252.1};
OS Haemophilus parahaemolyticus HK385.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=1095744 {ECO:0000313|EMBL:EIJ69252.1, ECO:0000313|Proteomes:UP000003016};
RN [1] {ECO:0000313|EMBL:EIJ69252.1, ECO:0000313|Proteomes:UP000003016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK385 {ECO:0000313|EMBL:EIJ69252.1,
RC ECO:0000313|Proteomes:UP000003016};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (FEB-2012) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIJ69252.1}.
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DR EMBL; AJSW01000043; EIJ69252.1; -; Genomic_DNA.
DR RefSeq; WP_005706993.1; NZ_UGHI01000002.1.
DR AlphaFoldDB; I3DC09; -.
DR GeneID; 78224847; -.
DR PATRIC; fig|1095744.4.peg.1453; -.
DR OrthoDB; 9179041at2; -.
DR Proteomes; UP000003016; Unassembled WGS sequence.
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 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 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 15..75
FT /note="HTH tetR-type"
FT /evidence="ECO:0000259|PROSITE:PS50977"
FT DNA_BIND 38..57
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00335"
SQ SEQUENCE 202 AA; 23164 MW; 4A4B4499D2EC9695 CRC64;
MSTLQVKMPK KTKAERQQQV LETLINELNS EGGMQRVTTE RLAKAVGVSE GALYRYFPSK
AKMFEALIEK IEQTLNSYVA ASKRRENGTE AIIKSIIYSV IEFARKNPGV TRILTGHALM
FEDDTLKARI AKFFYSLEIQ FSNILQMSKL HGGRAFDDER ALAAYLVNFC EGQFLRLVRS
NFNSSQYQPF EKQWAMLKPL FE
//
