ID   PRIB_YERE8              Reviewed;         106 AA.
AC   A1JIS9;
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=YE0393;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Binds single-stranded DNA at the primosome assembly site
CC       (PAS). {ECO:0000255|HAMAP-Rule:MF_00720}.
CC   -!- SUBUNIT: Component of the preprimosomal complex composed of PriA, PriB,
CC       PriC, DnaB and DnaT. 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; AM286415; CAL10520.1; -; Genomic_DNA.
DR   RefSeq; YP_001004766.1; NC_008800.1.
DR   AlphaFoldDB; A1JIS9; -.
DR   SMR; A1JIS9; -.
DR   STRING; 393305.YE0393; -.
DR   EnsemblBacteria; CAL10520; CAL10520; YE0393.
DR   KEGG; yen:YE0393; -.
DR   PATRIC; fig|393305.7.peg.487; -.
DR   eggNOG; COG2965; Bacteria.
DR   HOGENOM; CLU_166075_0_0_6; -.
DR   OMA; CQMPVII; -.
DR   Proteomes; UP000000642; 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.
FT   CHAIN           1..106
FT                   /note="Primosomal replication protein N"
FT                   /id="PRO_1000083302"
FT   DOMAIN          4..103
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00720"
SQ   SEQUENCE   106 AA;  11646 MW;  59505E37578DFF30 CRC64;
     MVTTNRLVLS GTVCKTPVRK VSPSGIPHCQ FVLEHRSTQQ EAGFSRQTWC RMPIIVSGQQ
     SQALTHSITV GSQLTVEGFI SCHQGRNGLN KLVLHAEQIE FIDSGD