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PRIB_NEIMB
ID   PRIB_NEIMB              Reviewed;         100 AA.
AC   Q9JZ30;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Primosomal replication protein N {ECO:0000255|HAMAP-Rule:MF_00720};
GN   Name=priB {ECO:0000255|HAMAP-Rule:MF_00720}; OrderedLocusNames=NMB1322;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(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; AE002098; AAF41697.1; -; Genomic_DNA.
DR   PIR; A81097; A81097.
DR   RefSeq; NP_274341.1; NC_003112.2.
DR   RefSeq; WP_002213304.1; NC_003112.2.
DR   AlphaFoldDB; Q9JZ30; -.
DR   SMR; Q9JZ30; -.
DR   STRING; 122586.NMB1322; -.
DR   PaxDb; Q9JZ30; -.
DR   EnsemblBacteria; AAF41697; AAF41697; NMB1322.
DR   KEGG; nme:NMB1322; -.
DR   PATRIC; fig|122586.8.peg.1658; -.
DR   HOGENOM; CLU_166075_1_2_4; -.
DR   OMA; HESWQKE; -.
DR   Proteomes; UP000000425; 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; Reference proteome.
FT   CHAIN           1..100
FT                   /note="Primosomal replication protein N"
FT                   /id="PRO_0000199055"
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
 
 
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