ID   PRIB_NEIM0              Reviewed;         100 AA.
AC   A9LZQ2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Primosomal replication protein N {ECO:0000255|HAMAP-Rule:MF_00720};
GN   Name=priB {ECO:0000255|HAMAP-Rule:MF_00720}; OrderedLocusNames=NMCC_1237;
OS   Neisseria meningitidis serogroup C (strain 053442).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=374833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=053442;
RX   PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004;
RA   Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z.,
RA   Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z.,
RA   Liang X., Xu J., Jin Q.;
RT   "Characterization of ST-4821 complex, a unique Neisseria meningitidis
RT   clone.";
RL   Genomics 91:78-87(2008).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00720}.
CC   -!- SUBUNIT: Homodimer. Component of the preprimosomal complex.
CC       {ECO:0000255|HAMAP-Rule:MF_00720}.
CC   -!- SIMILARITY: Belongs to the PriB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00720}.
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DR   EMBL; CP000381; ABX73410.1; -; Genomic_DNA.
DR   RefSeq; WP_012221739.1; NC_010120.1.
DR   AlphaFoldDB; A9LZQ2; -.
DR   SMR; A9LZQ2; -.
DR   EnsemblBacteria; ABX73410; ABX73410; NMCC_1237.
DR   KEGG; nmn:NMCC_1237; -.
DR   HOGENOM; CLU_166075_1_2_4; -.
DR   OMA; HESWQKE; -.
DR   Proteomes; UP000001177; Chromosome.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   DNA replication; DNA-binding; Primosome.
FT   CHAIN           1..100
FT                   /note="Primosomal replication protein N"
FT                   /id="PRO_1000083285"
FT   DOMAIN          1..99
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00720"
SQ   SEQUENCE   100 AA;  11618 MW;  A8CB0632D4DE1E33 CRC64;
     MGFNNLVSLA ALIEKVFPIR YTPAGISVLD IILKHESWQK ENGQQCFVQL EIPARILGRQ
     AEEWQYRQGV YVHVEGFLAQ KSRRSLMPML RIQNIKEYKG