ID   PRIB_NEIMF              Reviewed;         100 AA.
AC   A1KUE9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Primosomal replication protein N {ECO:0000255|HAMAP-Rule:MF_00720};
GN   Name=priB {ECO:0000255|HAMAP-Rule:MF_00720}; OrderedLocusNames=NMC1259;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
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; AM421808; CAM10492.1; -; Genomic_DNA.
DR   RefSeq; WP_002213304.1; NC_008767.1.
DR   AlphaFoldDB; A1KUE9; -.
DR   SMR; A1KUE9; -.
DR   EnsemblBacteria; CAM10492; CAM10492; NMC1259.
DR   KEGG; nmc:NMC1259; -.
DR   HOGENOM; CLU_166075_1_2_4; -.
DR   OMA; HESWQKE; -.
DR   OrthoDB; 1942216at2; -.
DR   Proteomes; UP000002286; 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_1000083286"
FT   DOMAIN          1..99
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00720"
SQ   SEQUENCE   100 AA;  11594 MW;  5AE2CAFDCCF16A50 CRC64;
     MGFNNLVSLA ALIEKVFPIR YTPAGIPVLD IILKHESWQE ENGQQCLVQL EIPARILGRQ
     AEEWQYRQGV YVHVEGFLAQ KSRRSLMPML RIQNIQEYKG