PRIB_ECOLI
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-AUG-2022, entry version 167.
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 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}.
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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 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 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; IC:ComplexPortal.
DR GO; GO:1990099; C:pre-primosome complex; IMP:UniProtKB.
DR GO; GO:1990077; C:primosome complex; IC: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; IC:ComplexPortal.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IC:ComplexPortal.
DR GO; GO:0006276; P:plasmid maintenance; IMP:EcoCyc.
DR GO; GO:0031297; P:replication fork processing; IC:ComplexPortal.
DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
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 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
