ID   DPO3A_CAMJE             Reviewed;        1200 AA.
AC   Q9PPI9; Q0PAG1;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=Cj0718;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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 (By similarity). {ECO:0000250}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL111168; CAL34855.1; -; Genomic_DNA.
DR   PIR; A81343; A81343.
DR   RefSeq; WP_002852165.1; NC_002163.1.
DR   RefSeq; YP_002344136.1; NC_002163.1.
DR   AlphaFoldDB; Q9PPI9; -.
DR   SMR; Q9PPI9; -.
DR   IntAct; Q9PPI9; 2.
DR   STRING; 192222.Cj0718; -.
DR   PaxDb; Q9PPI9; -.
DR   PRIDE; Q9PPI9; -.
DR   EnsemblBacteria; CAL34855; CAL34855; Cj0718.
DR   GeneID; 905036; -.
DR   KEGG; cje:Cj0718; -.
DR   PATRIC; fig|192222.6.peg.710; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_7; -.
DR   OMA; KQRFHLC; -.
DR   Proteomes; UP000000799; 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   3: Inferred from homology;
KW   Cytoplasm; DNA replication; DNA-directed DNA polymerase;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..1200
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103315"
SQ   SEQUENCE   1200 AA;  137341 MW;  17D40CA6623D34FC CRC64;
     MSQFTHLHLH TEYSLLDGAN KLKELALTLK EQGATSVAMT DHGNMFGAID FYQTMKAQGL
     KPIIGIEAYL HNHDELDDKS SRQRFHLCLY AKNEIGYQNL MYLSSQSYIK GLYYYPRINK
     KLLEDYSEGL ICSSACLQGE VNWHLNTYSE RNVRFGAKGY EAAKEAALWY KKVFKDDFYF
     EIMRHGIGDQ RMIDDDIIRL SKELNIKIIA TNDTHYTFKE RAAAHEVFMC IAMGKKLNDP
     DRMRHSVHEF YVKSPEQMSE LFADIPEAIE NTQEIAQKCN LELNLGNPTP PNFKFTREYA
     KDHNIILPEE TKEFSFDNDD MVFEELCKKG LEERLKFIDE SKHEEYKQRL EVEINIIKNM
     KFSGYMLIVH DFIKVAKDKG IPVGPGRGSA AGSLVSYCLR ITDLDPIPYS LLFERFLNPE
     RVSMPDIDVD FCQDRRAEVI DYVIDKYGAD KVAQVITFGK LLAKGVIRDV ARVCDMSIQD
     ADELAKLVPE ELKITLDAAY EKEPKIKEFI DRHPKGLEVW EYARALEGLN RNAGMHAAGV
     VISNESLWKK TPLFRQSKND ERHLVTQYSK DHLEDVDLIK FDFLGLKTLT VINNAIKLIK
     KRYNKDIIWE TIDVNDSKVY KTIQSGNTLG IFQIESGGMQ SLNARLKPER FEDIIAVLAL
     YRPGPMESGM LDDFIDRKHG LKSIEYPFDS LEKVLEPTYG VIVYQEQVMQ IVQIIGGFSL
     GGADVVRRAM GKKDPEKMKK LKTDFADGAE KQGYDRAKAE DLWELIVKFA GYGFNKSHSA
     AYALITFQTA YLKTYYPSEF MAALLTSEEN NVDKIAVYID EMKKMNIKLL PPSINKAIRE
     FSALEQDGKD AIIYGLGAIK SVGIPAVENL LEARQDGEFK DINDFLGKID PTKINRRTLE
     SLIKAGAFDE FGFTRKALFD NMENLSEASR KMAEVRKNAA SSLFGEEELT SGVQVNFTPK
     NEEFEVMEKL GYEKEILGIY VSGHPLDRFY EQINAIDYVK SLDFESLKNN GEILSIGKIE
     DFKSMMSKNN KRYGRIEILD YYSSFDATVF ESNVEEIENI IKDENLKNNA YGFVLGFKAE
     GGEKPSFFLK AIKDLQSLED GEIKAIKKFG AKKDFKNKEE NHFTAEPKEF EKNIIELDLT
     RLNRELIYEI HEIARNAHNP NEKNNKKLVL KVISAGSCLL YHTDFIISDS IVEEISNKYA