ID   DPO3A_CHLMU             Reviewed;        1237 AA.
AC   Q9PJJ7;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=TC_0832;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(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}.
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DR   EMBL; AE002160; AAF39632.1; -; Genomic_DNA.
DR   PIR; H81660; H81660.
DR   RefSeq; WP_010231707.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PJJ7; -.
DR   SMR; Q9PJJ7; -.
DR   STRING; 243161.TC_0832; -.
DR   EnsemblBacteria; AAF39632; AAF39632; TC_0832.
DR   GeneID; 1246200; -.
DR   KEGG; cmu:TC_0832; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_0; -.
DR   OMA; NECRRMG; -.
DR   OrthoDB; 561611at2; -.
DR   Proteomes; UP000000800; 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   InterPro; IPR010994; RuvA_2-like.
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; SSF47781; SSF47781; 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..1237
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103317"
SQ   SEQUENCE   1237 AA;  139894 MW;  5839D4F98D4CA223 CRC64;
     MTWIPLHCHS QYSILDATCS IKKFVAKAVE YHIPALALTD HGNLFGAVDF YKTCKQNAIK
     PIIGCELYVA PSSRFDKKKE RKSQVANHLI LLCKDEEGYR NLCLLSSLAY TEGFYYFPRI
     DRELLKQHSK GLICLSACLS GSIAQAALES EEALEKDLLW YQDLFQEDFF SEVQLHKSSE
     EKIALFEEEW LRQNYYQFIE KQLKVKDAVL TVSKRLGISS VATNDIHYLD PDDWLAHEIL
     LNVQSREPIR TAKQNTYVPN PKRKTYPSRE FYFKSPQEMA ELFADHPETI SNTLIVADRC
     NLELDFVTKH YPIYVPEDLQ KKGSYSEEER YNASSAFLEQ LCEQGLKTKY TPELLGHIAQ
     KFPEKDPLTV VKERLSLEST IIISKGMCDY LLIVWDIINW AKDHGIPVGP GRGSGAGSVM
     LFLLGITEIE PIRFDLFFER FINPERLSYP DIDIDICMIG REKVINYAIE RHGKENVAQI
     ITFGTMKAKM AIKDVGRTLD TPLSKVNLIA KKIPDLNATI ASALESDPDL RQLYIDDAEA
     AEIIDMAKKL EGSIRNTGVH AAGVIICGDP LTNHIPICVP KDSSMISTQY SMKPVESVGM
     LKVDFLGLKT LTSIHVATKA IYKKTGILLQ AATLPLNDRN TFSLLHQGKT MGIFQMESRG
     MQELAKNLRP DAFEEIIAIG ALYRPGPMDM IPSFINRKHG KENIEYDHPL MEPILKETFG
     IMVYQEQVMQ IAGSLAKYSL GEGDVLRRAM GKKDHEQMVK EREKFCSRAS ANGIDPSIAT
     TIFDKMEKFA SYGFNKSHAA AYGLITYTTA YLKANYPKEW LAALLTCDYD DIEKVGKLIQ
     EAHSMNIPVL PPDINESGQD FEATQEGIRF SLGAVKGVGV SIVDSIVEER EKNGPYRSLQ
     DFVQRSDFKK VTKKQLESLV DAGSFNCFEP NKDLAIAILN DLYDTFSREK KEAATGVLTF
     FSLNSMTKDP VKVTISPENI VRRSDKELLK REKELLGVYL TAHPMDAVKH LLPFLSVVQS
     KDFEGLPHGS VVRTVFLIDK VTTKISSVEH KKFALLQVSD EEDSYELPIW SDMYAEYQDL
     LEEDRLIYAI LTIDRRSDSL RLSCRWMRDL SSVNDTVITE CDEVYDRLKN QKIYSSTKKS
     TGGQSQAMVK KEEPKAIPPV TISLDLNRLR HSHLFTLKGL IRKYSGSRAL SLVFTKDNQR
     IASISPDSDF FVTEDISAFL QEIETTDIPA RILATAV