ID   DPO3A_HELPJ             Reviewed;        1211 AA.
AC   Q9ZJF9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=jhp_1353;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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}.
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DR   EMBL; AE001439; AAD06929.1; -; Genomic_DNA.
DR   PIR; C71817; C71817.
DR   RefSeq; WP_000662156.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZJF9; -.
DR   SMR; Q9ZJF9; -.
DR   STRING; 85963.jhp_1353; -.
DR   EnsemblBacteria; AAD06929; AAD06929; jhp_1353.
DR   KEGG; hpj:jhp_1353; -.
DR   PATRIC; fig|85963.30.peg.1198; -.
DR   eggNOG; COG0587; Bacteria.
DR   OMA; KQRFHLC; -.
DR   Proteomes; UP000000804; 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; Transferase.
FT   CHAIN           1..1211
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103324"
SQ   SEQUENCE   1211 AA;  138043 MW;  6DDA060F70465564 CRC64;
     MKENKAFTHL HLHTEYSLLD GANKIKILAK RIKELGMKSV SVTDHGNMFG AIDFYTSMKK
     EGIKPIIGME AYIHNDDNLS SKETKQRFHL CLFAKNQEGY ENLMFLSSMA YLEGFYYFPR
     INKKLLREHS KGIIASSACL QGEVNYHLNT NNERNRKYGA KGYDEAKRIA CEYQEIFEDD
     FYLEIMRHGI LDQRFIDEQV IKMSLETGLK IIATNDTHYT MPNDAKAQEV AMCVAMGKTL
     NDKGRLKHSV HEFYIKSPEE MAKLFADIPE ALENTQEIAD KCVLEIDLKD DKKNPPTPPS
     FKFTKAYAQN EGLSFEDDAS YFAHKAREGL RERLILVPEE KHEQYKERLE KEIEVITNMK
     FPGYMLIVWD FIRYAKEMGI PVGPGRGSAA GSLVAFALKI TDIDPLKYDL LFERFLNPER
     VSMPDIDTDF CQRRRKEIIE YMIEKYGKYN VAQVITFNKM LAKGVIRDVA RVLDMPYKEA
     DDFAKLIPNR LGITLKGYEK NGEFIEGAWE LEPKIKELVE SNEVAKQVWE YSLNLENLNR
     NAGVHAAALV VDSQKELWHK TPLFASEKTG GIVTQYSMKY LEPVDLIKFD FLGLKTLTVI
     DDALKIIKTQ HNIDVDFLSL DMDDPKVYKT IQSGDTVGIF QIESGMFQGL NKRLRPSSFE
     DIIAIIALGR PGPMESGMVD DFVNRKHGVE PIAYAFKELE PILKPTYGTI VYQEQVMQIV
     QTIGGFSLGE ADLIRRAMGK KDAQIMADNK AKFVEGAKNL GHDGQKAANL WDLIVKFAGY
     GFNKSHSAAY AMITFQTAYL KTYYKHEFMA AMLTSESNKI ESVARYIDEV RALEIEVMPP
     HINSSMQDFS VAEFKNQKGE LEKKIVFGLG AVKGVGGEPI KNIIEERAKG DYKSLEDFIS
     RVDFSKLTKK SLEPLVKSGS LDNLGYTRKT MLANLDLICD AGRAKDKANE MMQGGNSLFG
     AMEGGIKEQV VLDMVDLGEH DAKTLLECEY ETLGIHVSGN PLDEFKEEIK GFKNLVKSID
     IEELEIGSQA YLLGKIMEVK KKIGKRSGKP YGTADILDRY GKFELMLFEK QLNALEELDI
     NKPLVFKCKI EEQEEVARLR LFEILDLESA REVKIPKARY KDPEKQKEDV REIPPMEMLA
     SSSCSLAIVL ENDVKKEFLR QIKESALKHQ GKRPLYLIIK DKDKQFKIQS DLMVNEKIKD
     DFKGLEWRDL A