ID PRIB_ECOLI Reviewed; 104 AA. AC P07013; Q2M6A4; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 03-MAY-2023, entry version 170. DE RecName: Full=Primosomal replication protein N {ECO:0000255|HAMAP-Rule:MF_00720}; GN Name=priB {ECO:0000255|HAMAP-Rule:MF_00720}; GN OrderedLocusNames=b4201, JW4159; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3528756; DOI=10.1007/bf00330199; RA Schnier J., Kitakawa M., Isono K.; RT "The nucleotide sequence of an Escherichia coli chromosomal region RT containing the genes for ribosomal proteins S6, S18, L9 and an open reading RT frame."; RL Mol. Gen. Genet. 204:126-132(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=7610040; DOI=10.1093/nar/23.12.2105; RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.; RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region RT from 92.8 through 100 minutes."; RL Nucleic Acids Res. 23:2105-2119(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP PROTEIN SEQUENCE OF 2-28, AND FUNCTION. RC STRAIN=K12; RX PubMed=1856227; DOI=10.1016/s0021-9258(18)92800-0; RA Zavitz K.H., Digate R.J., Marians K.J.; RT "The priB and priC replication proteins of Escherichia coli. Genes, DNA RT sequence, overexpression, and purification."; RL J. Biol. Chem. 266:13988-13995(1991). RN [6] RP PROTEIN SEQUENCE OF 2-28, AND FUNCTION. RX PubMed=1646811; DOI=10.1016/s0021-9258(18)99000-9; RA Allen G.C. Jr., Kornberg A.; RT "The priB gene encoding the primosomal replication n protein of Escherichia RT coli."; RL J. Biol. Chem. 266:11610-11613(1991). RN [7] RP FUNCTION. RX PubMed=8366072; DOI=10.1016/s0021-9258(19)36500-7; RA Allen G.C. Jr., Kornberg A.; RT "Assembly of the primosome of DNA replication in Escherichia coli."; RL J. Biol. Chem. 268:19204-19209(1993). RN [8] RP SUBUNIT. RX PubMed=8663106; DOI=10.1074/jbc.271.26.15656; RA Liu J., Nurse P., Marians K.J.; RT "The ordered assembly of the phiX174-type primosome. III. PriB facilitates RT complex formation between PriA and DnaT."; RL J. Biol. Chem. 271:15656-15661(1996). RN [9] RP INDUCTION BY HYDROXYUREA. RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574; RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024; RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J., RA Walker G.C.; RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia RT coli."; RL Mol. Cell 36:845-860(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 ECO:0000269|PubMed:1646811, ECO:0000269|PubMed:1856227, CC ECO:0000269|PubMed:8366072}. 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 ECO:0000269|PubMed:8663106}. CC -!- INTERACTION: CC P07013; P0A8J2: dnaT; NbExp=4; IntAct=EBI-1125223, EBI-549621; CC P07013; P17888: priA; NbExp=3; IntAct=EBI-1125223, EBI-552050; CC P07013; P07013: priB; NbExp=4; IntAct=EBI-1125223, EBI-1125223; CC -!- INDUCTION: Induced by hydroxyurea. {ECO:0000269|PubMed:20005847}. CC -!- SIMILARITY: Belongs to the PriB family. {ECO:0000255|HAMAP- CC Rule:MF_00720, ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X04022; CAA27653.1; -; Genomic_DNA. DR EMBL; U14003; AAA97097.1; -; Genomic_DNA. DR EMBL; U00096; AAC77158.1; -; Genomic_DNA. DR EMBL; AP009048; BAE78202.1; -; Genomic_DNA. DR PIR; A30281; Q4ECFR. DR RefSeq; NP_418622.1; NC_000913.3. DR RefSeq; WP_001315977.1; NZ_LN832404.1. DR PDB; 1TXY; X-ray; 2.00 A; A/B=1-104. DR PDB; 1V1Q; X-ray; 2.10 A; A/B=1-102. DR PDB; 1WOC; X-ray; 2.00 A; A/B/C/D=2-104. DR PDB; 2CCZ; X-ray; 2.70 A; A/B=1-102. DR PDB; 2PNH; X-ray; 2.25 A; A/B=1-104. DR PDB; 5WQV; X-ray; 1.97 A; A/B=1-104. DR PDBsum; 1TXY; -. DR PDBsum; 1V1Q; -. DR PDBsum; 1WOC; -. DR PDBsum; 2CCZ; -. DR PDBsum; 2PNH; -. DR PDBsum; 5WQV; -. DR AlphaFoldDB; P07013; -. DR SMR; P07013; -. DR BioGRID; 4259640; 3. DR ComplexPortal; CPX-1951; Replication restart pre-primosome complex, priAB variant. DR ComplexPortal; CPX-5910; Replication restart primosome complex, priAB variant. DR DIP; DIP-10563N; -. DR IntAct; P07013; 12. DR MINT; P07013; -. DR STRING; 511145.b4201; -. DR jPOST; P07013; -. DR PaxDb; P07013; -. DR EnsemblBacteria; AAC77158; AAC77158; b4201. DR EnsemblBacteria; BAE78202; BAE78202; BAE78202. DR GeneID; 948722; -. DR KEGG; ecj:JW4159; -. DR KEGG; eco:b4201; -. DR PATRIC; fig|1411691.4.peg.2500; -. DR EchoBASE; EB0757; -. DR eggNOG; COG2965; Bacteria. DR HOGENOM; CLU_166075_0_0_6; -. DR OMA; CQMPVII; -. DR PhylomeDB; P07013; -. DR BioCyc; EcoCyc:EG10764-MON; -. DR BioCyc; MetaCyc:EG10764-MON; -. DR EvolutionaryTrace; P07013; -. DR PRO; PR:P07013; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:1990158; C:DnaB-DnaC-DnaT-PriA-PriB complex; NAS:ComplexPortal. DR GO; GO:1990099; C:pre-primosome complex; IMP:UniProtKB. DR GO; GO:1990077; C:primosome complex; NAS:ComplexPortal. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:EcoCyc. DR GO; GO:0006270; P:DNA replication initiation; IMP:EcoCyc. DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; NAS:ComplexPortal. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; NAS:ComplexPortal. DR GO; GO:0006276; P:plasmid maintenance; IMP:EcoCyc. DR GO; GO:0031297; P:replication fork processing; NAS:ComplexPortal. DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc. DR CDD; cd04496; SSB_OBF; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; Nucleic acid-binding proteins; 1. DR TIGRFAMs; TIGR04418; PriB_gamma; 1. DR PROSITE; PS50935; SSB; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; DNA replication; DNA-binding; KW Primosome; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1646811, FT ECO:0000269|PubMed:1856227" FT CHAIN 2..104 FT /note="Primosomal replication protein N" FT /id="PRO_0000199050" FT DOMAIN 2..101 FT /note="SSB" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00720" FT STRAND 3..20 FT /evidence="ECO:0007829|PDB:2CCZ" FT TURN 21..23 FT /evidence="ECO:0007829|PDB:2CCZ" FT STRAND 24..39 FT /evidence="ECO:0007829|PDB:2CCZ" FT STRAND 42..57 FT /evidence="ECO:0007829|PDB:2CCZ" FT HELIX 60..64 FT /evidence="ECO:0007829|PDB:2CCZ" FT STRAND 71..76 FT /evidence="ECO:0007829|PDB:2CCZ" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:2CCZ" FT STRAND 91..93 FT /evidence="ECO:0007829|PDB:2CCZ" FT STRAND 95..99 FT /evidence="ECO:0007829|PDB:2CCZ" SQ SEQUENCE 104 AA; 11442 MW; 0D52F9D68193B4AC CRC64; MTNRLVLSGT VCRAPLRKVS PSGIPHCQFV LEHRSVQEEA GFHRQAWCQM PVIVSGHENQ AITHSITVGS RITVQGFISC HKAKNGLSKM VLHAEQIELI DSGD //