ID   NOC_BACCQ               Reviewed;         290 AA.
AC   B9IT39;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=BCQ_5331;
OS   Bacillus cereus (strain Q1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=361100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q1;
RX   PubMed=19060151; DOI=10.1128/jb.01629-08;
RA   Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA   Xue Y., Zhu Y., Jin Q.;
RT   "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT   with industrial applications.";
RL   J. Bacteriol. 191:1120-1121(2009).
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; CP000227; ACM15727.1; -; Genomic_DNA.
DR   RefSeq; WP_000799029.1; NC_011969.1.
DR   AlphaFoldDB; B9IT39; -.
DR   SMR; B9IT39; -.
DR   EnsemblBacteria; ACM15727; ACM15727; BCQ_5331.
DR   KEGG; bcq:BCQ_5331; -.
DR   HOGENOM; CLU_023853_0_1_9; -.
DR   OMA; SQSYVAN; -.
DR   Proteomes; UP000000441; 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; Septation.
FT   CHAIN           1..290
FT                   /note="Nucleoid occlusion protein"
FT                   /id="PRO_1000189534"
FT   DNA_BIND        153..172
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02015"
SQ   SEQUENCE   290 AA;  33629 MW;  25821D591DCE2DA7 CRC64;
     MKNTFSRLFG FGDKESEFEL QDESHEEIDK KVYEEIQEIP IVNITPNRYQ PRTVFDDARI
     EELALTIRTH GLIQPIVVRQ YEDEKYEIIA GERRFRAATK LGWEKVPAII KNLNDTETAS
     VALIENLQRE ELTAIEEAVA YQKLIELHNL TQEALAQRLG KGQSTIANKL RLLKLPEEIK
     NALLEKSITE RHARALIPLK NEELQLKVLQ EIVEKQLNVK QTEERIAKLL EEAKPKRKAK
     QKAVSRDTRI AMNTIRQSLQ MVADSGLNVN SEEEEFDEYY QITIQIPKKK