HOLC_ECOLI
ID HOLC_ECOLI Reviewed; 147 AA.
AC P28905; P11649; Q2M650;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=DNA polymerase III subunit chi;
DE EC=2.7.7.7;
GN Name=holC; OrderedLocusNames=b4259, JW4216;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8389364; DOI=10.1016/s0021-9258(19)50266-6;
RA Xiao H., Crombie R., Dong Z., Onrust R., O'Donnell M.;
RT "DNA polymerase III accessory proteins. III. holC and holD encoding chi and
RT psi.";
RL J. Biol. Chem. 268:11773-11778(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-18.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8246893; DOI=10.1007/bf00284693;
RA Carter J.R., Franden M.A., Lippincott J., McHenry C.S.;
RT "Identification, molecular cloning and characterization of the gene
RT encoding the chi subunit of DNA polymerase III holoenzyme of Escherichia
RT coli.";
RL Mol. Gen. Genet. 241:399-408(1993).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102.
RC STRAIN=K12;
RX PubMed=2670557; DOI=10.1002/j.1460-2075.1989.tb03547.x;
RA Stirling C.J., Colloms S., Collins J.F., Szatmari G., Sherratt D.J.;
RT "xerB, an Escherichia coli gene required for plasmid ColE1 site-specific
RT recombination, is identical to pepA, encoding aminopeptidase A, a protein
RT with substantial similarity to bovine lens leucine aminopeptidase.";
RL EMBO J. 8:1623-1627(1989).
RN [7]
RP CHARACTERIZATION.
RX PubMed=8505305; DOI=10.1016/s0021-9258(19)50267-8;
RA Xiao H., Dong Z., O'Donnell M.;
RT "DNA polymerase III accessory proteins. IV. Characterization of chi and
RT psi.";
RL J. Biol. Chem. 268:11779-11784(1993).
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=2040637; DOI=10.1016/s0021-9258(18)99166-0;
RA Stukenberg P.T., Studwell-Vaughan P.S., O'Donnell M.;
RT "Mechanism of the sliding beta-clamp of DNA polymerase III holoenzyme.";
RL J. Biol. Chem. 266:11328-11334(1991).
RN [9]
RP REPLISOME COMPLEX, AND SUBUNIT.
RX PubMed=20413500; DOI=10.1126/science.1185757;
RA Reyes-Lamothe R., Sherratt D.J., Leake M.C.;
RT "Stoichiometry and architecture of active DNA replication machinery in
RT Escherichia coli.";
RL Science 328:498-501(2010).
RN [10]
RP REPLISOME COMPLEX, AND SUBUNIT.
RX PubMed=22157955; DOI=10.1038/nsmb.2179;
RA Georgescu R.E., Kurth I., O'Donnell M.E.;
RT "Single-molecule studies reveal the function of a third polymerase in the
RT replisome.";
RL Nat. Struct. Mol. Biol. 19:113-116(2011).
RN [11]
RP REVIEW.
RX PubMed=1575709; DOI=10.1002/bies.950140206;
RA O'Donnell M.;
RT "Accessory protein function in the DNA polymerase III holoenzyme from E.
RT coli.";
RL Bioessays 14:105-111(1992).
CC -!- FUNCTION: Part of the beta sliding clamp loading complex, which
CC hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA
CC replication pre-initiation complex (PubMed:2040637). DNA polymerase III
CC is a complex, multichain enzyme responsible for most of the replicative
CC synthesis in bacteria. This DNA polymerase also exhibits 3' to 5'
CC exonuclease activity. {ECO:0000269|PubMed:2040637}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC -!- SUBUNIT: The DNA polymerase III holoenzyme complex contains at least 10
CC different subunits organized into 3 functionally essential
CC subassemblies: the Pol III core, the beta sliding clamp processivity
CC factor and the clamp-loading complex. The Pol III core (subunits alpha,
CC epsilon and theta) contains the polymerase and the 3'-5' exonuclease
CC proofreading activities (PubMed:2040637). The polymerase is tethered to
CC the template via the dimeric beta sliding clamp processivity factor.
CC The clamp-loading complex (also called gamma complex) assembles the
CC beta sliding clamp onto the primed template and plays a central role in
CC the organization and communication at the replication fork. The clamp-
CC loading complex contains delta, delta', psi and chi, and 3 copies of
CC either or both of two different DnaX proteins, gamma and tau. The DNA
CC replisome complex has a single clamp loader (3 tau and 1 each of delta,
CC delta', psi and chi subunits) which binds 3 Pol III cores (1 core on
CC the leading strand and 2 on the lagging strand) each with a beta
CC sliding clamp dimer. Additional proteins in the replisome are other
CC copies of gamma, psi and chi, Ssb, DNA helicase and RNA primase
CC (PubMed:20413500, PubMed:22157955). The clamp loader hydrolyzes ATP to
CC assemble the beta processivity factor onto the primed template
CC (PubMed:2040637) and plays a central role in the organization and
CC communication at the replication fork. {ECO:0000269|PubMed:2040637,
CC ECO:0000269|PubMed:20413500, ECO:0000269|PubMed:22157955}.
CC -!- INTERACTION:
CC P28905; P06710: dnaX; NbExp=20; IntAct=EBI-549169, EBI-549140;
CC P28905; P28631: holB; NbExp=6; IntAct=EBI-549169, EBI-549161;
CC P28905; P28632: holD; NbExp=25; IntAct=EBI-549169, EBI-549176;
CC P28905; P0AGE0: ssb; NbExp=10; IntAct=EBI-549169, EBI-1118620;
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DR EMBL; L04574; AAA70368.1; -; Genomic_DNA.
DR EMBL; Z14155; CAA78524.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97156.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77216.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78256.1; -; Genomic_DNA.
DR EMBL; X15130; CAA33226.1; -; Genomic_DNA.
DR PIR; A46739; A46739.
DR RefSeq; NP_418680.1; NC_000913.3.
DR RefSeq; WP_000786400.1; NZ_LN832404.1.
DR PDB; 1EM8; X-ray; 2.10 A; A/C=1-147.
DR PDB; 3SXU; X-ray; 1.85 A; A=1-147.
DR PDBsum; 1EM8; -.
DR PDBsum; 3SXU; -.
DR AlphaFoldDB; P28905; -.
DR SMR; P28905; -.
DR BioGRID; 4262725; 159.
DR BioGRID; 853072; 5.
DR ComplexPortal; CPX-1926; DNA polymerase III clamp loader complex.
DR DIP; DIP-9933N; -.
DR IntAct; P28905; 41.
DR MINT; P28905; -.
DR STRING; 511145.b4259; -.
DR jPOST; P28905; -.
DR PaxDb; P28905; -.
DR PRIDE; P28905; -.
DR EnsemblBacteria; AAC77216; AAC77216; b4259.
DR EnsemblBacteria; BAE78256; BAE78256; BAE78256.
DR GeneID; 948787; -.
DR KEGG; ecj:JW4216; -.
DR KEGG; eco:b4259; -.
DR PATRIC; fig|1411691.4.peg.2445; -.
DR EchoBASE; EB1385; -.
DR eggNOG; COG2927; Bacteria.
DR HOGENOM; CLU_131584_0_0_6; -.
DR InParanoid; P28905; -.
DR OMA; WQFEPSA; -.
DR PhylomeDB; P28905; -.
DR BioCyc; EcoCyc:EG11413-MON; -.
DR BioCyc; MetaCyc:EG11413-MON; -.
DR BRENDA; 3.6.4.B8; 2026.
DR EvolutionaryTrace; P28905; -.
DR PRO; PR:P28905; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009360; C:DNA polymerase III complex; IC:ComplexPortal.
DR GO; GO:0043846; C:DNA polymerase III, clamp loader complex; IPI:ComplexPortal.
DR GO; GO:0030894; C:replisome; IC:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IC:ComplexPortal.
DR GO; GO:0006261; P:DNA-templated DNA replication; IC:ComplexPortal.
DR GO; GO:0032298; P:positive regulation of DNA-templated DNA replication initiation; IDA:EcoliWiki.
DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
DR Gene3D; 3.40.50.10110; -; 1.
DR InterPro; IPR007459; DNA_pol3_chi.
DR InterPro; IPR036768; PolIII_chi_sf.
DR PANTHER; PTHR38767; PTHR38767; 1.
DR Pfam; PF04364; DNA_pol3_chi; 1.
DR SUPFAM; SSF102400; SSF102400; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA replication;
KW DNA-directed DNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..147
FT /note="DNA polymerase III subunit chi"
FT /id="PRO_0000105517"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3SXU"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:3SXU"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:3SXU"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:3SXU"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:3SXU"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3SXU"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:3SXU"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:3SXU"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:3SXU"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:3SXU"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3SXU"
FT HELIX 124..136
FT /evidence="ECO:0007829|PDB:3SXU"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:3SXU"
SQ SEQUENCE 147 AA; 16633 MW; 7FEFFC359B28AA88 CRC64;
MKNATFYLLD NDTTVDGLSA VEQLVCEIAA ERWRSGKRVL IACEDEKQAY RLDEALWARP
AESFVPHNLA GEGPRGGAPV EIAWPQKRSS SRRDILISLR TSFADFATAF TEVVDFVPYE
DSLKQLARER YKAYRVAGFN LNTATWK
