ID   PRIB_NEIMA              Reviewed;         100 AA.
AC   Q9JU25; A1ISC6;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Primosomal replication protein N {ECO:0000255|HAMAP-Rule:MF_00720};
GN   Name=priB {ECO:0000255|HAMAP-Rule:MF_00720}; OrderedLocusNames=NMA1536;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
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; AL157959; CAM08682.1; -; Genomic_DNA.
DR   PIR; C81845; C81845.
DR   RefSeq; WP_010981204.1; NC_003116.1.
DR   AlphaFoldDB; Q9JU25; -.
DR   SMR; Q9JU25; -.
DR   EnsemblBacteria; CAM08682; CAM08682; NMA1536.
DR   KEGG; nma:NMA1536; -.
DR   HOGENOM; CLU_166075_1_2_4; -.
DR   OMA; HESWQKE; -.
DR   BioCyc; NMEN122587:NMA_RS07665-MON; -.
DR   Proteomes; UP000000626; 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_0000199054"
FT   DOMAIN          1..99
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00720"
SQ   SEQUENCE   100 AA;  11623 MW;  5AF4ADEBBD967C37 CRC64;
     MGFNNLVSLA VLIEKVFPIR YTPAGIPVLD IILKHESWQE ENGQQCLVQL EIPARILGRQ
     AEEWQYRQGV YVHVEGFLAQ KSRRSLMPML RIQNIQEYKG