NOC_BACSU
ID NOC_BACSU Reviewed; 283 AA.
AC P37524;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Nucleoid occlusion protein;
DE Short=Noc;
GN Name=noc; Synonyms=yyaA; OrderedLocusNames=BSU40990;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / CRK2000;
RX PubMed=1552862; DOI=10.1111/j.1365-2958.1992.tb01510.x;
RA Ogasawara N., Yoshikawa H.;
RT "Genes and their organization in the replication origin region of the
RT bacterial chromosome.";
RL Mol. Microbiol. 6:629-634(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP CHARACTERIZATION.
RX PubMed=11807071; DOI=10.1128/jb.184.4.1102-1111.2002;
RA Sievers J., Raether B., Perego M., Errington J.;
RT "Characterization of the parB-like yyaA gene of Bacillus subtilis.";
RL J. Bacteriol. 184:1102-1111(2002).
RN [5]
RP FUNCTION AS A COORDINATOR OF CELL DIVISION AND CHROMOSOME SEGREGATION,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=15210112; DOI=10.1016/j.cell.2004.06.002;
RA Wu L.J., Errington J.;
RT "Coordination of cell division and chromosome segregation by a nucleoid
RT occlusion protein in Bacillus subtilis.";
RL Cell 117:915-925(2004).
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:0000269|PubMed:15210112}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
CC {ECO:0000269|PubMed:15210112}.
CC -!- INDUCTION: Expressed constitutively. {ECO:0000269|PubMed:15210112}.
CC -!- SIMILARITY: Belongs to the ParB family. {ECO:0000305}.
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DR EMBL; X62539; CAA44406.1; -; Genomic_DNA.
DR EMBL; D26185; BAA05229.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16136.1; -; Genomic_DNA.
DR PIR; I40442; I40442.
DR RefSeq; NP_391979.1; NC_000964.3.
DR RefSeq; WP_003226829.1; NZ_JNCM01000034.1.
DR PDB; 6Y93; X-ray; 2.23 A; A/B=111-242.
DR PDB; 7OL9; X-ray; 2.90 A; A/B=1-242.
DR PDBsum; 6Y93; -.
DR PDBsum; 7OL9; -.
DR AlphaFoldDB; P37524; -.
DR SMR; P37524; -.
DR STRING; 224308.BSU40990; -.
DR jPOST; P37524; -.
DR PaxDb; P37524; -.
DR PRIDE; P37524; -.
DR EnsemblBacteria; CAB16136; CAB16136; BSU_40990.
DR GeneID; 937920; -.
DR KEGG; bsu:BSU40990; -.
DR PATRIC; fig|224308.179.peg.4441; -.
DR eggNOG; COG1475; Bacteria.
DR InParanoid; P37524; -.
DR OMA; SQSYVAN; -.
DR PhylomeDB; P37524; -.
DR BioCyc; BSUB:BSU40990-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
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:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0045881; P:positive regulation of sporulation resulting in formation of a cellular spore; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; DNA-binding;
KW Reference proteome; Septation.
FT CHAIN 1..283
FT /note="Nucleoid occlusion protein"
FT /id="PRO_0000178701"
FT DNA_BIND 148..167
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:6Y93"
FT HELIX 129..142
FT /evidence="ECO:0007829|PDB:6Y93"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:6Y93"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:6Y93"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:6Y93"
FT HELIX 172..179
FT /evidence="ECO:0007829|PDB:6Y93"
FT HELIX 185..191
FT /evidence="ECO:0007829|PDB:6Y93"
FT HELIX 197..210
FT /evidence="ECO:0007829|PDB:6Y93"
FT HELIX 214..228
FT /evidence="ECO:0007829|PDB:6Y93"
SQ SEQUENCE 283 AA; 32795 MW; BECF80CDB1FBCFB7 CRC64;
MKHSFSRFFG LGEKEQEPEI AEHDTNKEEI LEIPVNAIVP NRFQPRTIFS DEKIKELAMT
IHTHGIIQPI VVRHTEEEGQ YELIAGERRW RAVQSLEWEK IPAIIKDFSD TETASVALIE
NLQREELSSI EEAHAYARLL ELHDLTQEAL AQRLGKGQST IANKLRLLKL PQPVQEAIME
KKITERHARA LIPLKQPELQ VTLLTEIIEK SLNVKQTEDR VVKMLEQGQR KPKPRRKAFS
RDTRIAMNTI RQSLSMVEDS GVKLNTEEEE FEEYIQLTIR IPK
