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P0A988

- DPO3B_ECOLI

UniProt

P0A988 - DPO3B_ECOLI

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Protein
DNA polymerase III subunit beta
Gene
dnaN, b3701, JW3678
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The beta chain is required for initiation of replication; once it is clamped onto DNA it slides freely (bidirectional and ATP-independent) along duplex DNA. Coordinates protein traffic at the replication fork, where it interacts with multiple DNA polymerases.2 Publications

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

GO - Molecular functioni

  1. 3'-5' exonuclease activity Source: InterPro
  2. DNA binding Source: InterPro
  3. DNA-directed DNA polymerase activity Source: UniProtKB-KW
  4. identical protein binding Source: IntAct
  5. protein binding Source: UniProtKB

GO - Biological processi

  1. DNA strand elongation involved in DNA replication Source: EcoCyc
  2. cellular response to DNA damage stimulus Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication

Enzyme and pathway databases

BioCyciEcoCyc:EG10242-MONOMER.
ECOL316407:JW3678-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase III subunit beta (EC:2.7.7.7)
Alternative name(s):
Beta sliding clamp
Short name:
Beta clamp
Gene namesi
Name:dnaN
Ordered Locus Names:b3701, JW3678
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10242. dnaN.

Subcellular locationi

Cytoplasm
Note: Localizes to midcell position when chromosomes are condensed during DNA replication.1 Publication

GO - Cellular componenti

  1. DNA polymerase III complex Source: InterPro
  2. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi66 – 661G → E in dnaN159; a temperature- and UV-sensitive mutation, displays altered DNA polymerase usage, chronically induced SOS response; when associated with A-174. 1 Publication
Mutagenesisi174 – 1741G → A in dnaN159; a temperature- and UV-sensitive mutation, displays altered DNA polymerase usage, chronically induced SOS response; when associated with A-66. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 366366DNA polymerase III subunit beta
PRO_0000105434Add
BLAST

Proteomic databases

PaxDbiP0A988.
PRIDEiP0A988.

Expressioni

Gene expression databases

GenevestigatoriP0A988.

Interactioni

Subunit structurei

The DNA polymerase holoenzyme is a complex that contains 10 different types of subunits. These subunits are organized into 3 functionally essential subassemblies: the pol III core, the beta sliding clamp processivity factor and the clamp-loading complex. The pol III core (subunits alpha, epsilon and theta) contains the polymerase and the 3'-5' exonuclease proofreading activities. The polymerase is tethered to the template via the beta sliding clamp processivity factor (this entry). The clamp-loading complex assembles the beta processivity factor onto the primer template and plays a central role in the organization and communication at the replication fork. This complex contains delta, delta', psi and chi, and copies of either or both of two different DnaX proteins, gamma and tau. The composition of the holoenzyme is, therefore: (alpha,epsilon,theta)[2]-(gamma/tau)[3]-delta,delta', psi,chi-beta[4]. The beta chain is a homodimer when not associated with the other components. Can also be part of the RIDA complex (regulatory inactivation of DnaA), consisting of ATP-DnaA, ADP-Hda and DNA-loaded beta clamp. Probably also interacts with components of DNA polymerases I, II, IV and V. Binds to CrfC homooligomers at the midcell position during DNA replication.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself9EBI-542385,EBI-542385
dinBQ471552EBI-542385,EBI-1037359
dnaEP1044317EBI-542385,EBI-549111
dnaQP030076EBI-542385,EBI-549131
dnaXP067104EBI-542385,EBI-549140
hdaP699318EBI-542385,EBI-545453
holAP2863010EBI-542385,EBI-549153
rpeP0AG073EBI-542385,EBI-546020
tnsEP058454EBI-542385,EBI-2434514From a different organism.

Protein-protein interaction databases

DIPiDIP-36038N.
IntActiP0A988. 38 interactions.
STRINGi511145.b3701.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65
Helixi7 – 1711
Turni18 – 203
Beta strandi26 – 283
Helixi29 – 313
Beta strandi32 – 387
Beta strandi41 – 477
Beta strandi49 – 5810
Beta strandi66 – 716
Helixi72 – 8110
Beta strandi87 – 937
Beta strandi96 – 1016
Beta strandi104 – 1096
Helixi113 – 1153
Beta strandi126 – 1316
Helixi132 – 14211
Helixi143 – 1453
Helixi153 – 1564
Beta strandi157 – 1637
Beta strandi166 – 1727
Beta strandi174 – 18310
Beta strandi190 – 1956
Helixi197 – 2059
Beta strandi209 – 2113
Beta strandi213 – 2186
Beta strandi220 – 2278
Beta strandi230 – 2356
Helixi244 – 2463
Beta strandi254 – 2596
Helixi260 – 27112
Turni276 – 2783
Beta strandi280 – 2867
Beta strandi289 – 2957
Beta strandi301 – 3077
Beta strandi309 – 3124
Beta strandi315 – 3206
Helixi321 – 33111
Beta strandi334 – 3407
Beta strandi343 – 3453
Beta strandi347 – 3515
Beta strandi354 – 3618

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JQJX-ray2.90A/B1-366[»]
1JQLX-ray2.50A1-366[»]
1MMIX-ray1.85A/B1-366[»]
1OK7X-ray1.65A/B1-366[»]
1UNNX-ray1.90A/B1-366[»]
1WAImodel-A/B1-366[»]
2POLX-ray2.50A/B1-366[»]
2XURX-ray1.90A/B1-366[»]
3BEPX-ray1.92A/B1-366[»]
3D1EX-ray1.90A/B1-366[»]
3D1FX-ray2.00A/B1-366[»]
3D1GX-ray1.64A/B1-366[»]
3F1VX-ray1.77A/B1-366[»]
3PWEX-ray2.20A/B1-366[»]
3Q4JX-ray2.30A/B/C/D/E/F1-366[»]
3Q4KX-ray2.60A/B1-366[»]
3Q4LX-ray1.95A/B1-366[»]
3QSBX-ray1.90A/B1-366[»]
4K3KX-ray1.85A/B1-366[»]
4K3LX-ray1.50A/B1-366[»]
4K3MX-ray1.85A/B1-366[»]
4K3OX-ray2.00A/B1-366[»]
4K3PX-ray2.15A/B1-366[»]
4K3QX-ray1.85A/B1-366[»]
4K3RX-ray1.86A/B1-366[»]
4K3SX-ray1.75A/B1-366[»]
4MJPX-ray1.86A/B1-366[»]
4MJQX-ray1.73A/B1-366[»]
4MJRX-ray1.62A/B1-366[»]
4N94X-ray1.73A/B1-366[»]
4N95X-ray1.80A/B1-366[»]
4N96X-ray1.70A/B1-366[»]
4N97X-ray1.97A/B1-366[»]
4N98X-ray1.70A/B1-366[»]
4N99X-ray2.30A/B1-366[»]
4N9AX-ray1.90A/B1-366[»]
ProteinModelPortaliP0A988.
SMRiP0A988. Positions 1-366.

Miscellaneous databases

EvolutionaryTraceiP0A988.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 125125I
Add
BLAST
Regioni126 – 253128II
Add
BLAST
Regioni254 – 366113III
Add
BLAST

Phylogenomic databases

eggNOGiCOG0592.
HOGENOMiHOG000071791.
KOiK02338.
OMAiAVCSMPV.
OrthoDBiEOG65J53F.
PhylomeDBiP0A988.

Family and domain databases

InterProiIPR001001. DNA_polIII_beta.
IPR022635. DNA_polIII_beta_C.
IPR022637. DNA_polIII_beta_cen.
IPR022634. DNA_polIII_beta_N.
[Graphical view]
PfamiPF00712. DNA_pol3_beta. 1 hit.
PF02767. DNA_pol3_beta_2. 1 hit.
PF02768. DNA_pol3_beta_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000804. DNA_pol_III_b. 1 hit.
SMARTiSM00480. POL3Bc. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00663. dnan. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A988-1 [UniParc]FASTAAdd to Basket

« Hide

MKFTVEREHL LKPLQQVSGP LGGRPTLPIL GNLLLQVADG TLSLTGTDLE    50
MEMVARVALV QPHEPGATTV PARKFFDICR GLPEGAEIAV QLEGERMLVR 100
SGRSRFSLST LPAADFPNLD DWQSEVEFTL PQATMKRLIE ATQFSMAHQD 150
VRYYLNGMLF ETEGEELRTV ATDGHRLAVC SMPIGQSLPS HSVIVPRKGV 200
IELMRMLDGG DNPLRVQIGS NNIRAHVGDF IFTSKLVDGR FPDYRRVLPK 250
NPDKHLEAGC DLLKQAFARA AILSNEKFRG VRLYVSENQL KITANNPEQE 300
EAEEILDVTY SGAEMEIGFN VSYVLDVLNA LKCENVRMML TDSVSSVQIE 350
DAASQSAAYV VMPMRL 366
Length:366
Mass (Da):40,587
Last modified:April 1, 1988 - v1
Checksum:i7A45646F61255B5A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J01602 Genomic DNA. Translation: AAB59150.1.
L10328 Genomic DNA. Translation: AAA62052.1.
U00096 Genomic DNA. Translation: AAC76724.1.
AP009048 Genomic DNA. Translation: BAE77593.1.
M19876 Genomic DNA. Translation: AAA23695.1.
M13822 Genomic DNA. Translation: AAA24512.1.
K02179 Genomic DNA. Translation: AAA24510.1.
X04341 Genomic DNA. Translation: CAA27869.1.
PIRiA91510. DJEC3B.
RefSeqiNP_418156.1. NC_000913.3.
YP_491734.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76724; AAC76724; b3701.
BAE77593; BAE77593; BAE77593.
GeneIDi12930541.
948218.
KEGGiecj:Y75_p3472.
eco:b3701.
PATRICi32122899. VBIEscCol129921_3825.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J01602 Genomic DNA. Translation: AAB59150.1 .
L10328 Genomic DNA. Translation: AAA62052.1 .
U00096 Genomic DNA. Translation: AAC76724.1 .
AP009048 Genomic DNA. Translation: BAE77593.1 .
M19876 Genomic DNA. Translation: AAA23695.1 .
M13822 Genomic DNA. Translation: AAA24512.1 .
K02179 Genomic DNA. Translation: AAA24510.1 .
X04341 Genomic DNA. Translation: CAA27869.1 .
PIRi A91510. DJEC3B.
RefSeqi NP_418156.1. NC_000913.3.
YP_491734.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JQJ X-ray 2.90 A/B 1-366 [» ]
1JQL X-ray 2.50 A 1-366 [» ]
1MMI X-ray 1.85 A/B 1-366 [» ]
1OK7 X-ray 1.65 A/B 1-366 [» ]
1UNN X-ray 1.90 A/B 1-366 [» ]
1WAI model - A/B 1-366 [» ]
2POL X-ray 2.50 A/B 1-366 [» ]
2XUR X-ray 1.90 A/B 1-366 [» ]
3BEP X-ray 1.92 A/B 1-366 [» ]
3D1E X-ray 1.90 A/B 1-366 [» ]
3D1F X-ray 2.00 A/B 1-366 [» ]
3D1G X-ray 1.64 A/B 1-366 [» ]
3F1V X-ray 1.77 A/B 1-366 [» ]
3PWE X-ray 2.20 A/B 1-366 [» ]
3Q4J X-ray 2.30 A/B/C/D/E/F 1-366 [» ]
3Q4K X-ray 2.60 A/B 1-366 [» ]
3Q4L X-ray 1.95 A/B 1-366 [» ]
3QSB X-ray 1.90 A/B 1-366 [» ]
4K3K X-ray 1.85 A/B 1-366 [» ]
4K3L X-ray 1.50 A/B 1-366 [» ]
4K3M X-ray 1.85 A/B 1-366 [» ]
4K3O X-ray 2.00 A/B 1-366 [» ]
4K3P X-ray 2.15 A/B 1-366 [» ]
4K3Q X-ray 1.85 A/B 1-366 [» ]
4K3R X-ray 1.86 A/B 1-366 [» ]
4K3S X-ray 1.75 A/B 1-366 [» ]
4MJP X-ray 1.86 A/B 1-366 [» ]
4MJQ X-ray 1.73 A/B 1-366 [» ]
4MJR X-ray 1.62 A/B 1-366 [» ]
4N94 X-ray 1.73 A/B 1-366 [» ]
4N95 X-ray 1.80 A/B 1-366 [» ]
4N96 X-ray 1.70 A/B 1-366 [» ]
4N97 X-ray 1.97 A/B 1-366 [» ]
4N98 X-ray 1.70 A/B 1-366 [» ]
4N99 X-ray 2.30 A/B 1-366 [» ]
4N9A X-ray 1.90 A/B 1-366 [» ]
ProteinModelPortali P0A988.
SMRi P0A988. Positions 1-366.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-36038N.
IntActi P0A988. 38 interactions.
STRINGi 511145.b3701.

Proteomic databases

PaxDbi P0A988.
PRIDEi P0A988.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76724 ; AAC76724 ; b3701 .
BAE77593 ; BAE77593 ; BAE77593 .
GeneIDi 12930541.
948218.
KEGGi ecj:Y75_p3472.
eco:b3701.
PATRICi 32122899. VBIEscCol129921_3825.

Organism-specific databases

EchoBASEi EB0238.
EcoGenei EG10242. dnaN.

Phylogenomic databases

eggNOGi COG0592.
HOGENOMi HOG000071791.
KOi K02338.
OMAi AVCSMPV.
OrthoDBi EOG65J53F.
PhylomeDBi P0A988.

Enzyme and pathway databases

BioCyci EcoCyc:EG10242-MONOMER.
ECOL316407:JW3678-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A988.
PROi P0A988.

Gene expression databases

Genevestigatori P0A988.

Family and domain databases

InterProi IPR001001. DNA_polIII_beta.
IPR022635. DNA_polIII_beta_C.
IPR022637. DNA_polIII_beta_cen.
IPR022634. DNA_polIII_beta_N.
[Graphical view ]
Pfami PF00712. DNA_pol3_beta. 1 hit.
PF02767. DNA_pol3_beta_2. 1 hit.
PF02768. DNA_pol3_beta_3. 1 hit.
[Graphical view ]
PIRSFi PIRSF000804. DNA_pol_III_b. 1 hit.
SMARTi SM00480. POL3Bc. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00663. dnan. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structural analysis of the dnaA and dnaN genes of Escherichia coli."
    Ohmori H., Kimura M., Nagata T., Sakakibara Y.
    Gene 28:159-170(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
    Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
    Genomics 16:551-561(1993) [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. "Transcriptional organization of the dnaN and recF genes of Escherichia coli K-12."
    Armengod M.E.E., Garcca-Sogo M., Lambies E.
    J. Biol. Chem. 263:12109-12114(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
  6. "Overlapping arrangement of the recF and dnaN operons of Escherichia coli; positive and negative control sequences."
    Armengod M.E.E., Lambies E.
    Gene 43:183-196(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 143-170.
  7. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 297-366.
  8. "DNA sequence and transcription of the region upstream of the E. coli gyrB gene."
    Adachi T., Mizuuchi K., Menzel R., Gellert M.
    Nucleic Acids Res. 12:6389-6395(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 342-366.
  9. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  10. "Interaction of the sliding clamp beta-subunit and Hda, a DnaA-related protein."
    Kurz M., Dalrymple B., Wijffels G., Kongsuwan K.
    J. Bacteriol. 186:3508-3515(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDA.
  11. "The Escherichia coli dnaN159 mutant displays altered DNA polymerase usage and chronic SOS induction."
    Sutton M.D.
    J. Bacteriol. 186:6738-6748(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AT REPLICATION FORK, INTERACTION WITH DNAE, MUTAGENESIS OF GLY-66 AND GLY-174.
  12. "Hda monomerization by ADP binding promotes replicase clamp-mediated DnaA-ATP hydrolysis."
    Su'etsugu M., Nakamura K., Keyamura K., Kudo Y., Katayama T.
    J. Biol. Chem. 283:36118-36131(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN RIDA COMPLEX.
  13. "Evidence for roles of the Escherichia coli Hda protein beyond regulatory inactivation of DnaA."
    Baxter J.C., Sutton M.D.
    Mol. Microbiol. 85:648-668(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REPLICATION FORK.
  14. "A replicase clamp-binding dynamin-like protein promotes colocalization of nascent DNA strands and equipartitioning of chromosomes in E. coli."
    Ozaki S., Matsuda Y., Keyamura K., Kawakami H., Noguchi Y., Kasho K., Nagata K., Masuda T., Sakiyama Y., Katayama T.
    Cell Rep. 4:985-995(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CRFC, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  15. "Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp."
    Kong X.-P., Onrust R., O'Donnell M., Kuriyan J.
    Cell 69:425-437(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  16. "Flexibility revealed by the 1.85 A crystal structure of the beta sliding-clamp subunit of Escherichia coli DNA polymerase III."
    Oakley A.J., Prosselkov P., Wijffels G., Beck J.L., Wilce M.C., Dixon N.E.
    Acta Crystallogr. D 59:1192-1199(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
  17. "Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the beta-clamp."
    Bunting K.A., Roe S.M., Pearl L.H.
    EMBO J. 22:5883-5892(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH DINB.
  18. "Accessory protein function in the DNA polymerase III holoenzyme from E. coli."
    O'Donnell M.
    Bioessays 14:105-111(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiDPO3B_ECOLI
AccessioniPrimary (citable) accession number: P0A988
Secondary accession number(s): P00583, Q2M813
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: June 11, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The temperature- and UV-sensitive allele dnaN159 does not grow at higher than 37 degrees Celsius. The global SOS response is chronically induced. The UV-sensitivity of dnaN159 is dependent upon pol IV (dinB), it has an enhanced Pol V-dependent mutation rate (umuC, umuD), and is absolutely dependent on the polymerase activity of Pol I (polA) for viability.

Keywords - Technical termi

3D-structure, Complete proteome, 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

External Data

Dasty 3

Similar proteinsi