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Protein

Primosomal replication protein N

Gene

priB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds single-stranded DNA at the primosome assembly site (PAS). During primosome assembly it facilitates the complex formation between PriA and DnaT.UniRule annotation3 Publications

GO - Molecular functioni

  • single-stranded DNA binding Source: EcoCyc

GO - Biological processi

  • DNA replication, synthesis of RNA primer Source: UniProtKB-KW
  • DNA replication initiation Source: EcoCyc
  • plasmid maintenance Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

DNA replication

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10764-MONOMER.
ECOL316407:JW4159-MONOMER.
MetaCyc:EG10764-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Primosomal replication protein NUniRule annotation
Gene namesi
Name:priBUniRule annotation
Ordered Locus Names:b4201, JW4159
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10764. priB.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Primosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 104103Primosomal replication protein NPRO_0000199050Add
BLAST

Proteomic databases

PaxDbiP07013.

Expressioni

Inductioni

Induced by hydroxyurea.1 Publication

Interactioni

Subunit structurei

Component of the preprimosomal complex composed of one monomer of PriC and DnaT, two monomers of PriA, two dimers of PriB and one hexamer of DnaB. Upon transient interaction with DnaG it forms the primosome.UniRule annotation1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
dnaTP0A8J24EBI-1125223,EBI-549621
priAP178883EBI-1125223,EBI-552050

Protein-protein interaction databases

DIPiDIP-10563N.
IntActiP07013. 12 interactions.
STRINGi511145.b4201.

Structurei

Secondary structure

1
104
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1917Combined sources
Turni21 – 233Combined sources
Beta strandi25 – 3915Combined sources
Beta strandi42 – 5716Combined sources
Helixi60 – 634Combined sources
Beta strandi71 – 799Combined sources
Turni83 – 864Combined sources
Beta strandi91 – 999Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TXYX-ray2.00A/B1-104[»]
1V1QX-ray2.10A/B1-102[»]
1WOCX-ray2.00A/B/C/D2-104[»]
2CCZX-ray2.70A/B1-102[»]
2PNHX-ray2.25A/B1-104[»]
ProteinModelPortaliP07013.
SMRiP07013. Positions 2-101.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07013.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 101100SSBUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the PriB family.UniRule annotationCurated
Contains 1 SSB domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108VDV. Bacteria.
COG2965. LUCA.
HOGENOMiHOG000261221.
KOiK02686.
OMAiCQMPVII.
OrthoDBiEOG6KMB8F.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00720. PriB.
InterProiIPR012340. NA-bd_OB-fold.
IPR000424. Primosome_PriB/ssb.
IPR023646. Prisomal_replication_PriB.
[Graphical view]
PfamiPF00436. SSB. 1 hit.
[Graphical view]
PIRSFiPIRSF003135. Primosomal_n. 1 hit.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR04418. PriB_gamma. 1 hit.
PROSITEiPS50935. SSB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07013-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNRLVLSGT VCRAPLRKVS PSGIPHCQFV LEHRSVQEEA GFHRQAWCQM
60 70 80 90 100
PVIVSGHENQ AITHSITVGS RITVQGFISC HKAKNGLSKM VLHAEQIELI

DSGD
Length:104
Mass (Da):11,442
Last modified:January 23, 2007 - v3
Checksum:i0D52F9D68193B4AC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04022 Genomic DNA. Translation: CAA27653.1.
U14003 Genomic DNA. Translation: AAA97097.1.
U00096 Genomic DNA. Translation: AAC77158.1.
AP009048 Genomic DNA. Translation: BAE78202.1.
PIRiA30281. Q4ECFR.
RefSeqiNP_418622.1. NC_000913.3.
WP_001315977.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77158; AAC77158; b4201.
BAE78202; BAE78202; BAE78202.
GeneIDi948722.
KEGGiecj:JW4159.
eco:b4201.
PATRICi32123977. VBIEscCol129921_4333.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04022 Genomic DNA. Translation: CAA27653.1.
U14003 Genomic DNA. Translation: AAA97097.1.
U00096 Genomic DNA. Translation: AAC77158.1.
AP009048 Genomic DNA. Translation: BAE78202.1.
PIRiA30281. Q4ECFR.
RefSeqiNP_418622.1. NC_000913.3.
WP_001315977.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TXYX-ray2.00A/B1-104[»]
1V1QX-ray2.10A/B1-102[»]
1WOCX-ray2.00A/B/C/D2-104[»]
2CCZX-ray2.70A/B1-102[»]
2PNHX-ray2.25A/B1-104[»]
ProteinModelPortaliP07013.
SMRiP07013. Positions 2-101.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10563N.
IntActiP07013. 12 interactions.
STRINGi511145.b4201.

Proteomic databases

PaxDbiP07013.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77158; AAC77158; b4201.
BAE78202; BAE78202; BAE78202.
GeneIDi948722.
KEGGiecj:JW4159.
eco:b4201.
PATRICi32123977. VBIEscCol129921_4333.

Organism-specific databases

EchoBASEiEB0757.
EcoGeneiEG10764. priB.

Phylogenomic databases

eggNOGiENOG4108VDV. Bacteria.
COG2965. LUCA.
HOGENOMiHOG000261221.
KOiK02686.
OMAiCQMPVII.
OrthoDBiEOG6KMB8F.

Enzyme and pathway databases

BioCyciEcoCyc:EG10764-MONOMER.
ECOL316407:JW4159-MONOMER.
MetaCyc:EG10764-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP07013.
PROiP07013.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00720. PriB.
InterProiIPR012340. NA-bd_OB-fold.
IPR000424. Primosome_PriB/ssb.
IPR023646. Prisomal_replication_PriB.
[Graphical view]
PfamiPF00436. SSB. 1 hit.
[Graphical view]
PIRSFiPIRSF003135. Primosomal_n. 1 hit.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR04418. PriB_gamma. 1 hit.
PROSITEiPS50935. SSB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of an Escherichia coli chromosomal region containing the genes for ribosomal proteins S6, S18, L9 and an open reading frame."
    Schnier J., Kitakawa M., Isono K.
    Mol. Gen. Genet. 204:126-132(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "The priB and priC replication proteins of Escherichia coli. Genes, DNA sequence, overexpression, and purification."
    Zavitz K.H., Digate R.J., Marians K.J.
    J. Biol. Chem. 266:13988-13995(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-28, FUNCTION.
    Strain: K12.
  6. "The priB gene encoding the primosomal replication n protein of Escherichia coli."
    Allen G.C. Jr., Kornberg A.
    J. Biol. Chem. 266:11610-11613(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-28, FUNCTION.
  7. "Assembly of the primosome of DNA replication in Escherichia coli."
    Allen G.C. Jr., Kornberg A.
    J. Biol. Chem. 268:19204-19209(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The ordered assembly of the phiX174-type primosome. III. PriB facilitates complex formation between PriA and DnaT."
    Liu J., Nurse P., Marians K.J.
    J. Biol. Chem. 271:15656-15661(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  9. "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia coli."
    Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J., Walker G.C.
    Mol. Cell 36:845-860(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY HYDROXYUREA.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.

Entry informationi

Entry nameiPRIB_ECOLI
AccessioniPrimary (citable) accession number: P07013
Secondary accession number(s): Q2M6A4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.