ID A0A370G360_GLULI Unreviewed; 1142 AA.
AC A0A370G360;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN Name=dnaE {ECO:0000313|EMBL:MBB2186518.1};
GN ORFNames=C7453_104126 {ECO:0000313|EMBL:RDI38185.1}, HLH32_08975
GN {ECO:0000313|EMBL:MBB2186518.1};
OS Gluconacetobacter liquefaciens (Acetobacter liquefaciens).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconacetobacter.
OX NCBI_TaxID=89584 {ECO:0000313|EMBL:RDI38185.1, ECO:0000313|Proteomes:UP000254958};
RN [1] {ECO:0000313|EMBL:RDI38185.1, ECO:0000313|Proteomes:UP000254958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5603 {ECO:0000313|EMBL:RDI38185.1,
RC ECO:0000313|Proteomes:UP000254958};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB2186518.1, ECO:0000313|Proteomes:UP000562982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 1382 {ECO:0000313|EMBL:MBB2186518.1,
RC ECO:0000313|Proteomes:UP000562982};
RA Sombolestani A.;
RT "Description of novel Gluconacetobacter.";
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00025611}.
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 Evidence={ECO:0000256|ARBA:ARBA00024632};
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
CC complex. {ECO:0000256|ARBA:ARBA00026073}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC subfamily. {ECO:0000256|ARBA:ARBA00009496}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDI38185.1}.
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; JABEQI010000004; MBB2186518.1; -; Genomic_DNA.
DR EMBL; QQAW01000004; RDI38185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370G360; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000254958; Unassembled WGS sequence.
DR Proteomes; UP000562982; Unassembled WGS sequence.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd07433; PHP_PolIIIA_DnaE1; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 1.10.10.1600; Bacterial DNA polymerase III alpha subunit, thumb domain; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 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; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR InterPro; IPR049821; PolIIIA_DnaE1_PHP.
DR NCBIfam; TIGR00594; polc; 1.
DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR PANTHER; PTHR32294:SF0; DNA POLYMERASE III SUBUNIT ALPHA; 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 Pfam; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:MBB2186518.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:MBB2186518.1}.
FT DOMAIN 7..74
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1142 AA; 125230 MW; 9D76BF4734EF6C8D CRC64;
MSYADFVHLR VHSAYSLSQG AIRVADIAGM AKDMRMPAVA ITDTGNLFGA LEFSQYCSGK
GVQPIIGCQI ALPPRGDKPG LPVEPVVLLA QDDVGLMNLQ YLSSQGFLQG DTAEPTVSLE
MLCARAEGLI LLTGGTRGPL FRLLADGQQD EAGRLLETLH EAFGDRLAVE LHRHGLPVEQ
AVEPGMIALA DRLGLPLVAT NECFFPNPAM YEAHDALLCI AQGRTIAERD RWRVTPEHWF
KPPEMMRELF ADLPEACDNT LAIARRCAVR VETRKPLLPV CPKVQPGATE EETLRAMAAE
GLENRLARMT MDDATRQVYR ERLTFELDII AKMGFPGYFM IVADFIQWAK AHDIPVGPGR
GSGAGSLAAW ALTITDIDPI PFNLLFERFL NPERVSMPDF DIDFCQDRRD EVIRYVRGEY
GPDRVAQIIT FGKLQARAAV RDVGRVLGLP FGMVNKVAEL IPNNPAKPVT LKQAIEGEPR
LQEMRDDDEA IRRLLEIGQQ LEGLYRHAST HAAGVVIGDR QLVELVPLYR DPKSDMLVTQ
YNMKFVEQAG LVKFDFLGLT TLTILQRAVQ FLKGLGETVE LSALPLDDAL TYEMLARGDT
GGVFQFEGAG MRDVLKQMRP TRLEDLIAAV ALYRPGPMAN IPDYCRRKHG EAWEPPHEEI
RSILEETYGI MVYQEQVMQI AQKMAGYSLG GADLLRRAMG KKIRAEMDTQ REIFTEGAVG
RGIDREKAVE VFDLMAKFAD YGFNKSHAAA YALVSYQTAW MKANHPVPFL AACMSLAREK
TDKLAALRQE AERLGIPVLP PDINASGPDF TVERLADGRL GIRYALAAVK KVGFSAMEAL
VVSRGGRRFS DLADMAARVD PRQLNKMQIE NLAKAGAFDS ITPNRRLVAA AAETVLRRAN
AQAEEAASGQ IGLFGGGGAT AEPEPLRLPD VVDWPEFERL GMEAEAIGFH LTAHPLDSYG
PLLRRLGAVR ATGLEAAAQA GLTRVKIAGC VVDRKERPTR TGSKMAWVRL SDSSGGCEVT
LFSEVLSRTR EILTAGSAIL VTADLRLDGE ALRITASEVV SLEQAAAEAA AELRIWFDRE
DSVPPIHDIL ADSRGGRGKV VLLPSVAETR DVEVTLRGAY RVTPRMAQAI RAVAGVARVE
QA
//
