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 06-MAR-2007, entry version 66. DE Primosomal replication protein n. GN Name=priB; OrderedLocusNames=b4201, JW4159; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=86310297; 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 MEDLINE=95334362; 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 MEDLINE=97426617; 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 277:1453-1474(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 MEDLINE=91310687; 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 MEDLINE=91268023; 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 MEDLINE=93374896; 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 MEDLINE=96279088; 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). 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. 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. CC -!- SIMILARITY: Belongs to the priB family. CC -!- SIMILARITY: Contains 1 SSB domain. 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 PDB; 1TXY; X-ray; A/B=1-104. DR PDB; 1V1Q; X-ray; A/B=1-104. DR PDB; 1WOC; X-ray; A/B/C/D=1-104. DR PDB; 2CCZ; X-ray; A/B=-. DR DIP; DIP:10563N; -. DR IntAct; P07013; -. DR GenomeReviews; U00096_GR; b4201. DR GenomeReviews; AP009048_GR; JW4159. DR KEGG; ecj:JW4159; -. DR KEGG; eco:b4201; -. DR EchoBASE; EB0757; -. DR EcoGene; EG10764; priB. DR BioCyc; EcoCyc:EG10764-MONOMER; -. DR GO; GO:0003697; F:single-stranded DNA binding; IEA:HAMAP. DR HAMAP; MF_00720; -; 1. DR InterPro; IPR008994; OB_fold_NA_bd. DR InterPro; IPR012340; OB_NA_bd_sub. DR InterPro; IPR000424; SSB_primosomal_n. DR InterPro; IPR010913; ssDNA_bd. DR Gene3D; G3DSA:2.40.50.140; NA-bind_OB_sub; 1. DR Pfam; PF00436; SSB; 1. DR PROSITE; PS50935; SSB; 1. KW 3D-structure; Complete proteome; Direct protein sequencing; KW DNA replication; DNA-binding; Primosome. FT INIT_MET 1 1 Removed. FT CHAIN 2 104 Primosomal replication protein n. FT /FTId=PRO_0000199050. FT DOMAIN 2 101 SSB. FT STRAND 3 19 FT TURN 21 22 FT STRAND 25 39 FT TURN 40 41 FT STRAND 42 57 FT TURN 58 59 FT HELIX 60 63 FT TURN 64 65 FT TURN 68 69 FT STRAND 71 79 FT STRAND 91 99 SQ SEQUENCE 104 AA; 11442 MW; 0D52F9D68193B4AC CRC64; MTNRLVLSGT VCRAPLRKVS PSGIPHCQFV LEHRSVQEEA GFHRQAWCQM PVIVSGHENQ AITHSITVGS RITVQGFISC HKAKNGLSKM VLHAEQIELI DSGD //