NOC_BACMK
ID NOC_BACMK Reviewed; 290 AA.
AC A9VTL7;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 75.
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};
GN OrderedLocusNames=BcerKBAB4_5274;
OS Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBAB4;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
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; CP000903; ABY46417.1; -; Genomic_DNA.
DR RefSeq; WP_002016471.1; NC_010184.1.
DR AlphaFoldDB; A9VTL7; -.
DR SMR; A9VTL7; -.
DR STRING; 315730.BcerKBAB4_5274; -.
DR EnsemblBacteria; ABY46417; ABY46417; BcerKBAB4_5274.
DR GeneID; 66264962; -.
DR KEGG; bwe:BcerKBAB4_5274; -.
DR eggNOG; COG1475; Bacteria.
DR HOGENOM; CLU_023853_0_1_9; -.
DR OMA; SQSYVAN; -.
DR Proteomes; UP000002154; 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_0000346628"
FT DNA_BIND 153..172
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02015"
SQ SEQUENCE 290 AA; 33468 MW; D9F6FFCD9E165E5A CRC64;
MKNTFSRLFG FGDKESEFEL QDESHEEIAK KVYEEIQEIP IVNITPNRYQ PRTVFDDARI
EELALTIRTH GLIQPIVVRQ YEDDKYEIIA GERRFRAATK LGWEKVPAII KNLNDTETAS
VALIENLQRE ELTAIEEAVA YQKLIELHNL TQEALAQRLG KGQSTVANKL RLLKLPEEIK
SALLEKSITE RHARALIPLK NEELQLKVLQ EIVEKQLNVK QTEERIAKLL EEVKPKRKAK
QKAVSRDARI AMNTIRQSLQ MVANSGLNVN SAEEEFDEYY QITIKIPKKK