ID   PRIB_SALPA              Reviewed;         104 AA.
AC   Q5PJ57;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, 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=SPA4209;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV79946.1; -; Genomic_DNA.
DR   RefSeq; WP_001519453.1; NC_006511.1.
DR   AlphaFoldDB; Q5PJ57; -.
DR   SMR; Q5PJ57; -.
DR   EnsemblBacteria; AAV79946; AAV79946; SPA4209.
DR   GeneID; 66758616; -.
DR   KEGG; spt:SPA4209; -.
DR   HOGENOM; CLU_166075_0_0_6; -.
DR   OMA; CQMPVII; -.
DR   Proteomes; UP000008185; 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..104
FT                   /note="Primosomal replication protein N"
FT                   /id="PRO_1000083289"
FT   DOMAIN          1..101
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00720"
SQ   SEQUENCE   104 AA;  11414 MW;  9C69E7288F735AA2 CRC64;
     MTNRLALSGT VCRAPLRKVS PSGIPHCQFV LEHRSVQEEA GFHRQAWCQM PVIVSGHENQ
     AITHSITVGS RITVQGFISC HKAKNGLSKM VLHAEQIELI DSGD