NOC_ALKHC
ID NOC_ALKHC Reviewed; 283 AA.
AC Q9K5M9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Nucleoid occlusion protein {ECO:0000255|HAMAP-Rule:MF_02015};
DE Short=Noc {ECO:0000255|HAMAP-Rule:MF_02015};
GN Name=noc {ECO:0000255|HAMAP-Rule:MF_02015}; OrderedLocusNames=BH4059;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
CC -!- FUNCTION: Effects nucleoid occlusion by binding relatively
CC nonspecifically to DNA and preventing the assembly of the division
CC machinery in the vicinity of the nucleoid, especially under conditions
CC that disturb the cell cycle. It helps to coordinate cell division and
CC chromosome segregation by preventing the formation of the Z ring
CC through the nucleoid, which would cause chromosome breakage.
CC {ECO:0000255|HAMAP-Rule:MF_02015}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP-
CC Rule:MF_02015}.
CC -!- SIMILARITY: Belongs to the ParB family. {ECO:0000255|HAMAP-
CC Rule:MF_02015}.
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DR EMBL; BA000004; BAB07778.1; -; Genomic_DNA.
DR PIR; C84157; C84157.
DR RefSeq; WP_010900183.1; NC_002570.2.
DR AlphaFoldDB; Q9K5M9; -.
DR SMR; Q9K5M9; -.
DR STRING; 272558.10176684; -.
DR EnsemblBacteria; BAB07778; BAB07778; BAB07778.
DR KEGG; bha:BH4059; -.
DR eggNOG; COG1475; Bacteria.
DR HOGENOM; CLU_023853_0_1_9; -.
DR OMA; SQSYVAN; -.
DR OrthoDB; 653368at2; -.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR HAMAP; MF_02015; ParB_Noc; 1.
DR InterPro; IPR041468; HTH_ParB/Spo0J.
DR InterPro; IPR023705; Nucleoid_occlusion_protein.
DR InterPro; IPR004437; ParB/RepB/Spo0J.
DR InterPro; IPR003115; ParB/Sulfiredoxin_dom.
DR InterPro; IPR036086; ParB/Sulfiredoxin_sf.
DR Pfam; PF17762; HTH_ParB; 1.
DR Pfam; PF02195; ParBc; 1.
DR SMART; SM00470; ParB; 1.
DR SUPFAM; SSF110849; SSF110849; 1.
DR TIGRFAMs; TIGR04285; nucleoid_noc; 1.
DR TIGRFAMs; TIGR00180; parB_part; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cytoplasm; DNA-binding; Reference proteome;
KW Septation.
FT CHAIN 1..283
FT /note="Nucleoid occlusion protein"
FT /id="PRO_0000346623"
FT DNA_BIND 143..162
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02015"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 283 AA; 32673 MW; EA0F88C67D369F37 CRC64;
MKQPFSRLFG FGDKQDQEME TGKQEEVHQL PIKEIVPNRF QPRTIFDDER IEELAQTIRT
HGIIQPIVVR QREGKYEIIA GERRFRAVTL LGWETIPAII KEFNDSQTAS VALIENLQRE
GLTAVEEAVA YQKLIELHGL TQESLAQRLG KGQSTIANKL RLLHLSEPVQ QAIMERKISE
RHARALLSLK DDALETKLLE EIVEQHLNVK QTEERVKELL EDAPASKPKK KPTRKAYSKD
MRIAMNTIRQ SVDMVMKSGL KVDTAEEEHE DFYQFTIRIP KKK