PRIB_NEIG1
ID PRIB_NEIG1 Reviewed; 100 AA.
AC Q5F924;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Primosomal replication protein N {ECO:0000255|HAMAP-Rule:MF_00720, ECO:0000305};
DE AltName: Full=Primosome protein PriB {ECO:0000303|PubMed:19906704};
GN Name=priB {ECO:0000255|HAMAP-Rule:MF_00720, ECO:0000303|PubMed:19906704};
GN ORFNames=NGO_0582 {ECO:0000312|EMBL:AAW89313.1};
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231 {ECO:0000312|EMBL:AAW89313.1};
RN [1] {ECO:0000312|Proteomes:UP000000535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000312|Proteomes:UP000000535};
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND INTERACTION WITH PRIA.
RX PubMed=21861872; DOI=10.1186/1471-2180-11-189;
RA Feng C., Sunchu B., Greenwood M.E., Lopper M.E.;
RT "A bacterial PriB with weak single-stranded DNA binding activity can
RT stimulate the DNA unwinding activity of its cognate PriA helicase.";
RL BMC Microbiol. 11:189-189(2011).
RN [3] {ECO:0007744|PDB:3K8A}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), DNA-BINDING, INTERACTION WITH PRIA,
RP SUBUNIT, AND MUTAGENESIS OF TYR-21; LYS-34; GLU-41 AND LYS-81.
RX PubMed=19906704; DOI=10.1093/nar/gkp1031;
RA Dong J., George N.P., Duckett K.L., DeBeer M.A., Lopper M.E.;
RT "The crystal structure of Neisseria gonorrhoeae PriB reveals mechanistic
RT differences among bacterial DNA replication restart pathways.";
RL Nucleic Acids Res. 38:499-509(2010).
CC -!- FUNCTION: Stimulates the DNA unwinding activity of PriA helicase, which
CC does not seem to require single-stranded DNA-binding by PriB. Activates
CC DNA-dependent ATP hydrolysis catalyzed by PriA (PubMed:21861872). Has a
CC weak single-stranded DNA-binding activity (PubMed:21861872,
CC PubMed:19906704). Binds weakly also double-stranded DNA, a partial
CC duplex DNA with a 3' single-stranded DNA overhang, and a forked DNA
CC structure with fully duplex leading and lagging strand arms in vitro
CC (PubMed:21861872). {ECO:0000269|PubMed:19906704,
CC ECO:0000269|PubMed:21861872}.
CC -!- SUBUNIT: Homodimer (PubMed:19906704). Component of the preprimosomal
CC complex (By similarity). Interacts with PriA with high affinity,
CC independent of DNA presence (PubMed:21861872, PubMed:19906704).
CC {ECO:0000250|UniProtKB:P07013, ECO:0000269|PubMed:19906704,
CC ECO:0000269|PubMed:21861872}.
CC -!- SIMILARITY: Belongs to the PriB family. {ECO:0000255|HAMAP-
CC Rule:MF_00720, ECO:0000305}.
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DR EMBL; AE004969; AAW89313.1; -; Genomic_DNA.
DR RefSeq; WP_003692950.1; NC_002946.2.
DR RefSeq; YP_207725.1; NC_002946.2.
DR PDB; 3K8A; X-ray; 2.70 A; A/B=1-100.
DR PDBsum; 3K8A; -.
DR AlphaFoldDB; Q5F924; -.
DR SMR; Q5F924; -.
DR STRING; 242231.NGO_0582; -.
DR DNASU; 3282384; -.
DR EnsemblBacteria; AAW89313; AAW89313; NGO_0582.
DR KEGG; ngo:NGO_0582; -.
DR PATRIC; fig|242231.10.peg.688; -.
DR HOGENOM; CLU_166075_1_2_4; -.
DR OMA; HESWQKE; -.
DR EvolutionaryTrace; Q5F924; -.
DR Proteomes; UP000000535; Chromosome.
DR GO; GO:1990099; C:pre-primosome complex; ISS:UniProtKB.
DR GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:UniProtKB.
DR GO; GO:0051096; P:positive regulation of helicase activity; IDA:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00720; PriB; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000424; Primosome_PriB/ssb.
DR InterPro; IPR023646; Prisomal_replication_PriB.
DR PIRSF; PIRSF003135; Primosomal_n; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR04418; PriB_gamma; 1.
DR PROSITE; PS50935; SSB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; Primosome; Reference proteome.
FT CHAIN 1..100
FT /note="Primosomal replication protein N"
FT /id="PRO_0000436555"
FT DOMAIN 4..99
FT /note="SSB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00252"
FT MUTAGEN 21
FT /note="Y->A: 1.3-fold lower single-stranded DNA-binding
FT activity than wild-type."
FT /evidence="ECO:0000269|PubMed:19906704"
FT MUTAGEN 34
FT /note="K->A: Significantly lower single-stranded DNA-
FT binding activity. No effect on the levels of DNA unwinding
FT activity of PriA."
FT /evidence="ECO:0000269|PubMed:19906704"
FT MUTAGEN 41
FT /note="E->A: 3.4-fold higher single-stranded DNA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:19906704"
FT MUTAGEN 81
FT /note="K->A: Significantly lower single-stranded DNA-
FT binding activity."
FT /evidence="ECO:0000269|PubMed:19906704"
FT STRAND 5..16
FT /evidence="ECO:0007829|PDB:3K8A"
FT STRAND 27..41
FT /evidence="ECO:0007829|PDB:3K8A"
FT STRAND 44..57
FT /evidence="ECO:0007829|PDB:3K8A"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:3K8A"
FT STRAND 71..84
FT /evidence="ECO:0007829|PDB:3K8A"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:3K8A"
SQ SEQUENCE 100 AA; 11445 MW; 873F595F5DFCF363 CRC64;
MGFTNLVSLA ALIEKAFPIR YTPAGIPVLD IILKHESWQE ENGQQCLVQL EIPARILGRQ
AEEWQYRQGD CATVEGFLAQ KSRRSLMPML RIQNIKEYKG
