ID   PRIB_ECO8A              Reviewed;         104 AA.
AC   B7M9G3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Primosomal replication protein N {ECO:0000255|HAMAP-Rule:MF_00720};
GN   Name=priB {ECO:0000255|HAMAP-Rule:MF_00720}; OrderedLocusNames=ECIAI1_4434;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928160; CAR01176.1; -; Genomic_DNA.
DR   RefSeq; WP_001296681.1; NC_011741.1.
DR   AlphaFoldDB; B7M9G3; -.
DR   SMR; B7M9G3; -.
DR   GeneID; 66671886; -.
DR   KEGG; ecr:ECIAI1_4434; -.
DR   HOGENOM; CLU_166075_0_0_6; -.
DR   OMA; CQMPVII; -.
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_1000132619"
FT   DOMAIN          1..101
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00720"
SQ   SEQUENCE   104 AA;  11472 MW;  6622ED9395C2F1B8 CRC64;
     MTNRLVLSGT VCRTPLRKVS PSGIPHCQFV LEHRSVQEEA GFHRQAWCQM PVIVSGHENQ
     AITHSITVGS RITVQGFISC HKAKNGLSKM VLHAEQIELI DSGD