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Primosomal replication protein N (Primosome protein PriB)

 PRIB_NEIG1              Reviewed;         100 AA.
Q5F924;
06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
15-MAR-2005, sequence version 1.
07-JUN-2017, entry version 84.
RecName: Full=Primosomal replication protein N {ECO:0000255|HAMAP-Rule:MF_00720, ECO:0000305};
AltName: Full=Primosome protein PriB {ECO:0000303|PubMed:19906704};
Name=priB {ECO:0000255|HAMAP-Rule:MF_00720,
ECO:0000303|PubMed:19906704};
ORFNames=NGO_0582 {ECO:0000312|EMBL:AAW89313.1};
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
Neisseriaceae; Neisseria.
NCBI_TaxID=242231 {ECO:0000312|EMBL:AAW89313.1};
[1] {ECO:0000312|Proteomes:UP000000535}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700825 / FA 1090 {ECO:0000312|Proteomes:UP000000535};
Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
"The complete genome sequence of Neisseria gonorrhoeae.";
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[2]
FUNCTION, AND INTERACTION WITH PRIA.
PubMed=21861872; DOI=10.1186/1471-2180-11-189;
Feng C., Sunchu B., Greenwood M.E., Lopper M.E.;
"A bacterial PriB with weak single-stranded DNA binding activity can
stimulate the DNA unwinding activity of its cognate PriA helicase.";
BMC Microbiol. 11:189-189(2011).
[3] {ECO:0000244|PDB:3K8A}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), DNA-BINDING, INTERACTION WITH
PRIA, SUBUNIT, AND MUTAGENESIS OF TYR-21; LYS-34; GLU-41 AND LYS-81.
PubMed=19906704; DOI=10.1093/nar/gkp1031;
Dong J., George N.P., Duckett K.L., DeBeer M.A., Lopper M.E.;
"The crystal structure of Neisseria gonorrhoeae PriB reveals
mechanistic differences among bacterial DNA replication restart
pathways.";
Nucleic Acids Res. 38:499-509(2010).
-!- FUNCTION: Stimulates the DNA unwinding activity of PriA helicase,
which does not seem to require single-stranded DNA-binding by
PriB. Activates DNA-dependent ATP hydrolysis catalyzed by PriA
(PubMed:21861872). Has a weak single-stranded DNA-binding activity
(PubMed:21861872, PubMed:19906704). Binds weakly also double-
stranded DNA, a partial duplex DNA with a 3' single-stranded DNA
overhang, and a forked DNA structure with fully duplex leading and
lagging strand arms in vitro (PubMed:21861872).
{ECO:0000269|PubMed:19906704, ECO:0000269|PubMed:21861872}.
-!- SUBUNIT: Homodimer (PubMed:19906704). Component of the
preprimosomal complex (By similarity). Interacts with PriA with
high affinity, independent of DNA presence (PubMed:21861872,
PubMed:19906704). {ECO:0000250|UniProtKB:P07013,
ECO:0000269|PubMed:19906704, ECO:0000269|PubMed:21861872}.
-!- SIMILARITY: Belongs to the PriB family. {ECO:0000255|HAMAP-
Rule:MF_00720, ECO:0000305}.
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EMBL; AE004969; AAW89313.1; -; Genomic_DNA.
RefSeq; WP_003692950.1; NC_002946.2.
RefSeq; YP_207725.1; NC_002946.2.
PDB; 3K8A; X-ray; 2.70 A; A/B=1-100.
PDBsum; 3K8A; -.
ProteinModelPortal; Q5F924; -.
SMR; Q5F924; -.
DNASU; 3282384; -.
EnsemblBacteria; AAW89313; AAW89313; NGO_0582.
GeneID; 3282384; -.
KEGG; ngo:NGO_0582; -.
PATRIC; fig|242231.10.peg.688; -.
HOGENOM; HOG000261222; -.
KO; K02686; -.
OMA; HESWQKE; -.
BioCyc; NGON242231:GI2G-553-MONOMER; -.
EvolutionaryTrace; Q5F924; -.
Proteomes; UP000000535; Chromosome.
GO; GO:1990099; C:pre-primosome complex; ISS:UniProtKB.
GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
GO; GO:0032781; P:positive regulation of ATPase activity; IDA:UniProtKB.
GO; GO:0051096; P:positive regulation of helicase activity; IDA:UniProtKB.
HAMAP; MF_00720; PriB; 1.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR000424; Primosome_PriB/ssb.
InterPro; IPR023646; Prisomal_replication_PriB.
PIRSF; PIRSF003135; Primosomal_n; 1.
SUPFAM; SSF50249; SSF50249; 1.
TIGRFAMs; TIGR04418; PriB_gamma; 1.
PROSITE; PS50935; SSB; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; DNA replication; DNA-binding;
Primosome; Reference proteome.
CHAIN 1 100 Primosomal replication protein N.
/FTId=PRO_0000436555.
DOMAIN 4 99 SSB. {ECO:0000255|PROSITE-
ProRule:PRU00252}.
MUTAGEN 21 21 Y->A: 1.3-fold lower single-stranded DNA-
binding activity than wild-type.
{ECO:0000269|PubMed:19906704}.
MUTAGEN 34 34 K->A: Significantly lower single-stranded
DNA-binding activity. No effect on the
levels of DNA unwinding activity of PriA.
{ECO:0000269|PubMed:19906704}.
MUTAGEN 41 41 E->A: 3.4-fold higher single-stranded
DNA-binding activity.
{ECO:0000269|PubMed:19906704}.
MUTAGEN 81 81 K->A: Significantly lower single-stranded
DNA-binding activity.
{ECO:0000269|PubMed:19906704}.
STRAND 5 16 {ECO:0000244|PDB:3K8A}.
STRAND 27 41 {ECO:0000244|PDB:3K8A}.
STRAND 44 57 {ECO:0000244|PDB:3K8A}.
HELIX 58 63 {ECO:0000244|PDB:3K8A}.
STRAND 71 84 {ECO:0000244|PDB:3K8A}.
STRAND 88 97 {ECO:0000244|PDB:3K8A}.
SEQUENCE 100 AA; 11445 MW; 873F595F5DFCF363 CRC64;
MGFTNLVSLA ALIEKAFPIR YTPAGIPVLD IILKHESWQE ENGQQCLVQL EIPARILGRQ
AEEWQYRQGD CATVEGFLAQ KSRRSLMPML RIQNIKEYKG


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