ID   DPO3A_MYCPN             Reviewed;         872 AA.
AC   P75404;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=MPN_378; ORFNames=MP459;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB96107.1; -; Genomic_DNA.
DR   PIR; S73785; S73785.
DR   RefSeq; NP_110066.1; NC_000912.1.
DR   RefSeq; WP_010874734.1; NC_000912.1.
DR   AlphaFoldDB; P75404; -.
DR   SMR; P75404; -.
DR   IntAct; P75404; 4.
DR   STRING; 272634.MPN_378; -.
DR   EnsemblBacteria; AAB96107; AAB96107; MPN_378.
DR   KEGG; mpn:MPN_378; -.
DR   PATRIC; fig|272634.6.peg.409; -.
DR   HOGENOM; CLU_001600_0_1_14; -.
DR   OMA; HTNSYYN; -.
DR   BioCyc; MPNE272634:G1GJ3-599-MON; -.
DR   Proteomes; UP000000808; 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   InterPro; IPR011708; DNA_pol3_alpha_NTPase_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; 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   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..872
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103327"
SQ   SEQUENCE   872 AA;  99257 MW;  25F8E365E2D058D7 CRC64;
     MFVNLHTNSY YNFLNSTLSP QKLVDLAVQD QQVAVCLTDP NLFGATEFFL ACQKAHIKPL
     IGLSVTVRHY EQNVNLLVIA QTNRGYQNLM CLALVKDQPD LQLEPFLDGN VVIICTQTEL
     RLNTANPVYL AHGLSGRYPK IAVTQKPVKC QNTNKDLTLL LTLKQISQIN SEHFQPLEWK
     LSRSLNEIQL DPPLLQQLRH QPFLSQKAAQ QIFSEEELGN LQKLVEQSQW DLTKLKASSL
     QVSHNDAQML SEQCQLALTE FLKLNPQLNK QLYEERLAKE LEIINSLHFA SYFLVVSDLV
     QFAHNNDILI GPGRGSAVGS LVAFLLKITQ IDPVANNLIF ERFISRHRQG LPDIDIDIME
     TKRDLVIDYV MQKYGREQCA QIVTFQKFKT RSALRDVGKV FNHIEGAEDL LGKLPKDKSL
     LELDVNGVTD PVLQLSLKSF RLLWEVAREI INFPRQPSIH ASGVVIVTEP LITTIPLMVG
     NNNNYVTQVS MDWLEWYNLN KFDLLGLINL TMIHEVVQAV KPKEVSVQQF LQQIPLDDEA
     TFTNLTNQAT LGVFQLESFG MKKVLKQIKP HNLHDLAIVL ALYRPGPQDN INTFIANRNL
     GFDTSDIDPR ILPILKETYG VLIFQEQVIN IAKTVANYSL ETADSFRRAI SKKNLQVIQD
     NMRSFYEGAL ANNFSLKAAT TIFNYIQRFA GYGFNLSHAL GYALLSYWTA WLKTHYFEQF
     NLWWLNHEQG KKEKQKQLLN EFISSGYEIC PPLINKAKSD FSVQDKKLYL GFKLINGIGD
     KQAHALEHVQ EVLKQNPNLS LIATVNLCLS KTVGGLELKD ITLLQQAGCF NCFNYTVDFN
     LAKSFWVQSN HELFPKIPLD QPPVINWKSF GF