ID   PRIB_SHIDS              Reviewed;         104 AA.
AC   Q328J8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Primosomal replication protein N {ECO:0000255|HAMAP-Rule:MF_00720};
GN   Name=priB {ECO:0000255|HAMAP-Rule:MF_00720}; OrderedLocusNames=SDY_4370;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Binds single-stranded DNA at the primosome assembly site
CC       (PAS). During primosome assembly it facilitates the complex formation
CC       between PriA and DnaT. {ECO:0000255|HAMAP-Rule:MF_00720}.
CC   -!- SUBUNIT: Component of the preprimosomal complex composed of one monomer
CC       of PriC and DnaT, two monomers of PriA, two dimers of PriB and one
CC       hexamer of DnaB. Upon transient interaction with DnaG it forms the
CC       primosome. {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; CP000034; ABB64257.1; -; Genomic_DNA.
DR   RefSeq; WP_011378947.1; NC_007606.1.
DR   RefSeq; YP_405748.1; NC_007606.1.
DR   AlphaFoldDB; Q328J8; -.
DR   SMR; Q328J8; -.
DR   STRING; 300267.SDY_4370; -.
DR   EnsemblBacteria; ABB64257; ABB64257; SDY_4370.
DR   KEGG; sdy:SDY_4370; -.
DR   PATRIC; fig|300267.13.peg.5159; -.
DR   HOGENOM; CLU_166075_0_0_6; -.
DR   OMA; CQMPVII; -.
DR   Proteomes; UP000002716; 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   CDD; cd04496; SSB_OBF; 1.
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   Pfam; PF00436; SSB; 1.
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..104
FT                   /note="Primosomal replication protein N"
FT                   /id="PRO_1000083300"
FT   DOMAIN          1..101
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00720"
SQ   SEQUENCE   104 AA;  11429 MW;  3722468925C2F1A4 CRC64;
     MTNRLVLSGT VCRTPLRKVS PSGIPHCQFV LEHRSVQEEA GFHRQAWCQM PVIVSGHENQ
     AITHSITVGS SITVQGFISC YKAKNGLSKM VLHAEQIELI DSGD