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SLMA_IDILO
ID   SLMA_IDILO              Reviewed;         196 AA.
AC   Q5QZB7;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Nucleoid occlusion factor SlmA {ECO:0000255|HAMAP-Rule:MF_01839};
GN   Name=slmA {ECO:0000255|HAMAP-Rule:MF_01839}; OrderedLocusNames=IL0237;
OS   Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA   Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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:0000255|HAMAP-Rule:MF_01839}.
CC   -!- SUBUNIT: Homodimer. Interacts with FtsZ. {ECO:0000255|HAMAP-
CC       Rule:MF_01839}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP-
CC       Rule:MF_01839}.
CC   -!- SIMILARITY: Belongs to the nucleoid occlusion factor SlmA family.
CC       {ECO:0000255|HAMAP-Rule:MF_01839}.
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DR   EMBL; AE017340; AAV81080.1; -; Genomic_DNA.
DR   RefSeq; WP_011233500.1; NC_006512.1.
DR   AlphaFoldDB; Q5QZB7; -.
DR   SMR; Q5QZB7; -.
DR   STRING; 283942.IL0237; -.
DR   EnsemblBacteria; AAV81080; AAV81080; IL0237.
DR   KEGG; ilo:IL0237; -.
DR   eggNOG; COG1309; Bacteria.
DR   HOGENOM; CLU_069356_5_0_6; -.
DR   OMA; IEQTVFG; -.
DR   OrthoDB; 1437290at2; -.
DR   Proteomes; UP000001171; 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   HAMAP; MF_01839; NO_factor_SlmA; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR001647; HTH_TetR.
DR   InterPro; IPR023769; NO_SlmA.
DR   Pfam; PF00440; TetR_N; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS50977; HTH_TETR_2; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; DNA-binding;
KW   Reference proteome.
FT   CHAIN           1..196
FT                   /note="Nucleoid occlusion factor SlmA"
FT                   /id="PRO_0000198972"
FT   DOMAIN          6..66
FT                   /note="HTH tetR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01839"
FT   DNA_BIND        29..48
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01839"
FT   COILED          108..135
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01839"
SQ   SEQUENCE   196 AA;  22566 MW;  49E19093368FA096 CRC64;
     MAEQKRNRRE EILQALAAML ETSPGQRITT AKLAANLGVS EAALYRHFPS KARMFEGLIE
     FVEDTLLTRI NMIMDEEKNT LSRCHAILQL LLTFAERNPG ITRVMTGDAL MGEHDRLRGR
     MEDLFNRIES SIKQILREKA MREQQRFIVD EAVLANLLLS YADGKISQFV RSNFKRLPTE
     HFSAQWQVME QQLISA
 
 
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