ID   PRIB_YERPS              Reviewed;         106 AA.
AC   Q66FA1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Primosomal replication protein N {ECO:0000255|HAMAP-Rule:MF_00720};
GN   Name=priB {ECO:0000255|HAMAP-Rule:MF_00720}; OrderedLocusNames=YPTB0439;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH19679.1; -; Genomic_DNA.
DR   RefSeq; WP_002210154.1; NC_006155.1.
DR   AlphaFoldDB; Q66FA1; -.
DR   SMR; Q66FA1; -.
DR   EnsemblBacteria; CAH19679; CAH19679; YPTB0439.
DR   GeneID; 66843144; -.
DR   KEGG; yps:YPTB0439; -.
DR   OMA; CQMPVII; -.
DR   Proteomes; UP000001011; 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_1000083306"
FT   DOMAIN          4..103
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00720"
SQ   SEQUENCE   106 AA;  11632 MW;  59505E205CE05EE0 CRC64;
     MVTTNRLVLS GTVCKTPVRK VSPSGIPHCQ FVLEHRSTQQ EAGFSRQTWC RMPIVVSGQQ
     SQALTHSITV GSQLTVEGFI SCHQGRNGLN KLVLHAEQIE FIDSGD