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 18-SEP-2019, entry version 153. 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; Proteobacteria; 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 RT reading 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., RA Blattner F.R.; RT "Analysis of the Escherichia coli genome VI: DNA sequence of the RT region 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., RA Mau B., 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 RT MG1655 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; RA Zavitz K.H., Digate R.J., Marians K.J.; RT "The priB and priC replication proteins of Escherichia coli. Genes, RT DNA 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; RA Allen G.C. Jr., Kornberg A.; RT "The priB gene encoding the primosomal replication n protein of RT Escherichia coli."; RL J. Biol. Chem. 266:11610-11613(1991). RN [7] RP FUNCTION. RX PubMed=8366072; 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 RT facilitates 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 RT Escherichia 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 CC formation 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 CC monomer of PriC and DnaT, two monomers of PriA, two dimers of PriB CC and one hexamer of DnaB. Upon transient interaction with DnaG it CC forms the primosome. {ECO:0000255|HAMAP-Rule:MF_00720, CC ECO:0000269|PubMed:8663106}. CC -!- INTERACTION: CC Self; NbExp=4; IntAct=EBI-1125223, EBI-1125223; CC P0A8J2:dnaT; NbExp=4; IntAct=EBI-1125223, EBI-549621; CC P17888:priA; NbExp=3; IntAct=EBI-1125223, EBI-552050; 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 SMR; P07013; -. DR BioGrid; 4259640; 3. DR ComplexPortal; CPX-1951; DnaB-DnaC-DnaT-PriA-PriB complex. DR DIP; DIP-10563N; -. DR IntAct; P07013; 12. DR MINT; P07013; -. DR STRING; 511145.b4201; -. DR PaxDb; P07013; -. DR PRIDE; 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 EcoGene; EG10764; priB. DR eggNOG; ENOG4108VDV; Bacteria. DR eggNOG; COG2965; LUCA. DR HOGENOM; HOG000261221; -. DR KO; K02686; -. DR BioCyc; EcoCyc:EG10764-MONOMER; -. DR BioCyc; ECOL316407:JW4159-MONOMER; -. DR BioCyc; MetaCyc:EG10764-MONOMER; -. DR EvolutionaryTrace; P07013; -. DR PRO; PR:P07013; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:1990099; C:pre-primosome complex; IMP:UniProtKB. 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; IEA:UniProtKB-KW. DR GO; GO:0006276; P:plasmid maintenance; IMP:EcoCyc. DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc. DR CDD; cd04496; SSB_OBF; 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 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW DNA replication; DNA-binding; Primosome; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1646811, FT ECO:0000269|PubMed:1856227}. FT CHAIN 2 104 Primosomal replication protein N. FT /FTId=PRO_0000199050. FT DOMAIN 2 101 SSB. {ECO:0000255|HAMAP-Rule:MF_00720}. FT STRAND 3 20 {ECO:0000244|PDB:2CCZ}. FT TURN 21 23 {ECO:0000244|PDB:2CCZ}. FT STRAND 24 39 {ECO:0000244|PDB:2CCZ}. FT STRAND 42 57 {ECO:0000244|PDB:2CCZ}. FT HELIX 60 64 {ECO:0000244|PDB:2CCZ}. FT STRAND 71 76 {ECO:0000244|PDB:2CCZ}. FT STRAND 84 86 {ECO:0000244|PDB:2CCZ}. FT STRAND 91 93 {ECO:0000244|PDB:2CCZ}. FT STRAND 95 99 {ECO:0000244|PDB:2CCZ}. SQ SEQUENCE 104 AA; 11442 MW; 0D52F9D68193B4AC CRC64; MTNRLVLSGT VCRAPLRKVS PSGIPHCQFV LEHRSVQEEA GFHRQAWCQM PVIVSGHENQ AITHSITVGS RITVQGFISC HKAKNGLSKM VLHAEQIELI DSGD //