ID A0A1B9ABH6_9BACI Unreviewed; 293 AA.
AC A0A1B9ABH6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Nucleoid occlusion protein {ECO:0000256|HAMAP-Rule:MF_02015};
DE Short=Noc {ECO:0000256|HAMAP-Rule:MF_02015};
GN Name=noc {ECO:0000256|HAMAP-Rule:MF_02015};
GN ORFNames=A8L44_16100 {ECO:0000313|EMBL:OCA81203.1};
OS Bacillus sp. FJAT-27986.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1743146 {ECO:0000313|EMBL:OCA81203.1, ECO:0000313|Proteomes:UP000092673};
RN [1] {ECO:0000313|EMBL:OCA81203.1, ECO:0000313|Proteomes:UP000092673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27986 {ECO:0000313|EMBL:OCA81203.1,
RC ECO:0000313|Proteomes:UP000092673};
RA Liu X., Pan Z., Shi H., Ge C., Che J., Lan J., Chen Q., Zhu Y., Wang J.,
RA Liu B., Liu G.;
RT "Bacillus sp. FJAT-27986.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_02015}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000256|HAMAP-
CC Rule:MF_02015}.
CC -!- SIMILARITY: Belongs to the ParB family. {ECO:0000256|ARBA:ARBA00006295,
CC ECO:0000256|HAMAP-Rule:MF_02015}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OCA81203.1}.
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DR EMBL; MAYV01000019; OCA81203.1; -; Genomic_DNA.
DR RefSeq; WP_066109711.1; NZ_MAYV01000019.1.
DR AlphaFoldDB; A0A1B9ABH6; -.
DR STRING; 1743146.A8L44_16100; -.
DR OrthoDB; 9802051at2; -.
DR Proteomes; UP000092673; Unassembled WGS sequence.
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 CDD; cd16393; SPO0J_N; 1.
DR Gene3D; 1.10.10.2830; -; 1.
DR Gene3D; 3.90.1530.30; -; 1.
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 NCBIfam; TIGR04285; nucleoid_noc; 1.
DR NCBIfam; TIGR00180; parB_part; 1.
DR PANTHER; PTHR33375; CHROMOSOME-PARTITIONING PROTEIN PARB-RELATED; 1.
DR PANTHER; PTHR33375:SF8; NUCLEOID OCCLUSION PROTEIN; 1.
DR Pfam; PF17762; HTH_ParB; 1.
DR Pfam; PF02195; ParBc; 1.
DR SMART; SM00470; ParB; 1.
DR SUPFAM; SSF109709; KorB DNA-binding domain-like; 1.
DR SUPFAM; SSF110849; ParB/Sulfiredoxin; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_02015};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_02015};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02015};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_02015}; Reference proteome {ECO:0000313|Proteomes:UP000092673};
KW Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_02015}.
FT DOMAIN 38..128
FT /note="ParB/Sulfiredoxin"
FT /evidence="ECO:0000259|SMART:SM00470"
FT DNA_BIND 154..173
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02015"
SQ SEQUENCE 293 AA; 33616 MW; A6FE86BE057961D7 CRC64;
MTKHPFSRFF GLGDKEQNVD RESEIETEKE EINHDEIHKL PISSIVPNRF QPRSIFDDEK
IEELALTIET HGIIQPIVVR EIHDGQFEII AGERRYRAIS KLGWDKIPAI INNLSDTETA
SVALIENLQR EELSPIEEAV AYSKLIELHQ LTQEGLANRL GIGQSTVANK IRLLKLPQVV
QNAVMQKAIT ERHARSLIPL KDPEKQAKLV EEIIDKGLNV KQTEERVNKL LSADEDKKPR
AIRKAFSKDM RIAVNTIRQS MSMVKDNGIN LDSEETEFDD FYQITIRIPK KRK
//