DPO3A_CAUVN
ID DPO3A_CAUVN Reviewed; 1143 AA.
AC B8GWS6;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=DNA polymerase III subunit alpha;
DE EC=2.7.7.7;
GN Name=dnaE1; Synonyms=dnaE; OrderedLocusNames=CCNA_02003;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF VAL-569.
RX PubMed=14762018; DOI=10.1128/jb.186.4.1205-1212.2004;
RA Lo T., van Der Schalie E., Werner T., Brun Y.V., Din N.;
RT "A temperature-sensitive mutation in the dnaE gene of Caulobacter
RT crescentus that prevents initiation of DNA replication but not ongoing
RT elongation of DNA.";
RL J. Bacteriol. 186:1205-1212(2004).
CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC responsible for most of the replicative synthesis in bacteria. This DNA
CC polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain
CC is the DNA polymerase. {ECO:0000269|PubMed:14762018}.
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: DNA polymerase III contains a core (composed of alpha, epsilon
CC and theta chains) that associates with a tau subunit. This core
CC dimerizes to form the PolIII' complex. PolIII' associates with the
CC gamma complex (composed of gamma, delta, delta', psi and chi chains)
CC and with the beta chain to form the complete DNA polymerase III complex
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC subfamily. {ECO:0000305}.
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DR EMBL; CP001340; ACL95468.1; -; Genomic_DNA.
DR RefSeq; WP_010919792.1; NC_011916.1.
DR RefSeq; YP_002517376.1; NC_011916.1.
DR AlphaFoldDB; B8GWS6; -.
DR SMR; B8GWS6; -.
DR PRIDE; B8GWS6; -.
DR EnsemblBacteria; ACL95468; ACL95468; CCNA_02003.
DR GeneID; 7333331; -.
DR KEGG; ccs:CCNA_02003; -.
DR PATRIC; fig|565050.3.peg.1962; -.
DR HOGENOM; CLU_001600_0_0_5; -.
DR OMA; KQRFHLC; -.
DR OrthoDB; 561611at2; -.
DR PhylomeDB; B8GWS6; -.
DR Proteomes; UP000001364; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.1600; -; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR041931; DNA_pol3_alpha_thumb_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR InterPro; IPR004805; PolC_alpha.
DR PANTHER; PTHR32294; PTHR32294; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 1.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; SSF89550; 1.
DR TIGRFAMs; TIGR00594; polc; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA replication; DNA-directed DNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..1143
FT /note="DNA polymerase III subunit alpha"
FT /id="PRO_0000378286"
FT MUTAGEN 569
FT /note="V->E: Temperature-sensitive. Blocks the initiation
FT stage of DNA replication and still allows DNA elongation to
FT occur, but at a reduced rate, with the mutated protein
FT being only partially active at 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:14762018"
SQ SEQUENCE 1143 AA; 125539 MW; 445F362DCC7DB92B CRC64;
MSDAEGQGFV HLRVRSAYSL LEGAIKADQI GKLAAEAKMP AAGLADRANL FGALEYSSYA
KDAGVQPIIG CAIPVVGIGG GPTERWARAP TLMLLAQNER GYLNLSELSS IAYLDSAELP
EPVVPWAKVA EHSEGLILLS GGTDGPVDAL FAAGKTAEAS AALAEMHRVF GDRFYVELQR
HGLPRQAAAE PGLVNWAYDH DVPLVATNDV YFAKPGFYDA HDALLCISDG AFVGQDERRR
VTPEHWFKPA EEMRKLFADL PEACDNTLDI ARRCAFMVHK RDPILPSFPT GDGRNEAEEL
EHQAREGLKM RLEGLTLSAP EEEYWKRLDF ELGIIKKMGF PGYFLIVSDF IKWGKAHGIP
VGPGRGSGAG SLVAWVLTIT DLDPLRFGLL FERFLNPERV SMPDFDVDFC QERREEVISY
VQEKYGRDRV AQIITFGSLQ ARAVLRDVGR VMQLPLGLVD RLCKMVPNNP AAPVTLAQAI
DLEPRLKQAK KEDANVSACL DVALQLEGLF RNASTHAAGL VIGDRPLTQL TPLYKDPRSD
LPATQFNMKW VESAGLVKFD FLGLKTLTVL DRAVKHLKKR GFEIDLGKLP FDDAKTYELL
ASGQTVGVFQ LESQGMRDTL RKMRCGSIEE ITALISLYRP GPMDNIDTFV DCKFGRKPVD
TLHPSLEAVL KETYGVIVYQ EQVMQIAQIL AGYSLGEADL LRRAMGKKKK EEMDLQKIRF
VSGAKEKNVP EEQSGSIFEL VAKFAGYGFN KSHAAAYAFI SYQTAWLKAN TPVEFFAASM
SLDLSNTDKL AVFHQDARRF GITVRAPDVN RSGADFEVEN GEVLYALGAI RNVGLEAMKH
LVAVRAEGGP FRDVFDFVER IDPRQVNKRA IENLARAGAF DSIHKNRAQI VASADVLIAH
AQSCHADRQG GQGGLFGSDP GAGRPRLSKT ENWNQVDLLD EELSAVGFYL TGHPLEDMVG
MLRRRRTVML AEAMAQAEAG AEAFRMCGVV RRRQERASQS GEKFAFVSLS DPTGEYEVLY
PPESLRKCRD VLEPGKAVAI KVRAKARDGE VRFFGDDAEP IEKAVENVVA GLRVHLSPSA
AEIDALKRRL EPAQAQKGGE VTFVAAIGGG REIELRLPGR YTLDAALRGA LKTAPGVALL
EDV
