ID   DPO3A_CHLTR             Reviewed;        1237 AA.
AC   O84549;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=CT_545;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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; AE001273; AAC68147.1; -; Genomic_DNA.
DR   PIR; B71501; B71501.
DR   RefSeq; NP_220060.1; NC_000117.1.
DR   RefSeq; WP_010725247.1; NC_000117.1.
DR   AlphaFoldDB; O84549; -.
DR   SMR; O84549; -.
DR   STRING; 813.O172_03000; -.
DR   EnsemblBacteria; AAC68147; AAC68147; CT_545.
DR   GeneID; 884322; -.
DR   KEGG; ctr:CT_545; -.
DR   PATRIC; fig|272561.5.peg.592; -.
DR   HOGENOM; CLU_001600_0_0_0; -.
DR   InParanoid; O84549; -.
DR   OMA; NECRRMG; -.
DR   Proteomes; UP000000431; 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; Reference proteome; Transferase.
FT   CHAIN           1..1237
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103319"
SQ   SEQUENCE   1237 AA;  139545 MW;  D5E165A05514E77F CRC64;
     MTWIPLHCHS QYSILDATCS IKKFVAKAVE YQIPALALTD HGNLFGAVEF YKTCKQNAIK
     PIIGCELYVA PSSRFDKKKE RKSRVANHLI LLCKDEEGYR NLCLLSSLAY TEGFYYVPRI
     DRDLLSQHSK GLICLSACLS GSVAQAALES EEDLEKDLLW YQDLFQEDFF SEVQLHKSSE
     EKVALFEETW LKQNYYQFIE KQLKVNEAVL ATSKRLGIPS VATNDIHYLN PDDWLAHEIL
     LNVQSREPIR TAKQNTYIPN PKRKTYPSRE FYFKSPQEIA ELFAAHPETI TNTCIVAERC
     HLELDFETKH YPIYVPEALQ KKGSYTEEER YKASSAFLEE LCEQGLTSKY TPELLGHIAK
     KFPGEDPLTL VKERLKLESS IIISKGMCDY LLIVWDIINW AKDHGIPVGP GRGSGAGSVM
     LFLLGITEIE PIRFDLFFER FINPERISYP DIDIDICMIG RERVINYAIE RHGKDNVAQI
     ITFGTMKAKM AIKDVGRTLD TPLAKVNFIA KHIPDLNATI TSALEADPEL RQLYVDDAEA
     AEVIDMAKKL EGSIRNTGVH AAGVIICGDP LTNHIPICVP KDSSMISTQY SMKPVESVGM
     LKVDFLGLKT LTGIHIATQA IYKKTGILLR AATIPLDDQN TFSLLHQGKT MGIFQMESRG
     MQDLAKNLRP DAFEEIIAIG ALYRPGPMDM IPSFINRKHG KENIEYDHPL MEPILKETFG
     IMVYQEQVMQ IAGSLAKYSL GEGDVLRRAM GKKDHEQMVK EREKFCSRAA ANGIDPSIAT
     TIFDKMEKFA SYGFNKSHAA AYGLITYTTA YLKANYPKEW LAALLTCDYD DIEKVGKLIQ
     EAHSMNILVL PPDINESGQD FEATQKGIRF SLGAVKGVGM SIVDSIVEER EKNGPYKSLQ
     DFVQRADFKK VTKKQLENLV DAGTFDCFEP NKDLALAILN DLYDTFSREK KEAATGVLTF
     FSLDSMARDP VKITVSPENV IQRSPKELLK REKELLGVYL TAHPMDAVEH MLPFLSVVPA
     RDFEGLPHGT IIRTVFLIDK VTTKISSAEQ KKFALLQVSD EVDSYELPIW ADMYAEYRDL
     LEEDRLIYAI LAIDRRSDSL RLSCRWMRDL STVNDSVIAE CDEVYDRLKS QKVYSSTKKS
     TGAQSSAMIK KVETREISPV TISLDLNKLR HSHLFILKGL IRKYSGSQAL SLVFTKDNQR
     FASISPDADF FVTDDISSLL QEIEATNIPA RVLATTV