ID A0A3P1VE77_9STRE Unreviewed; 1034 AA.
AC A0A3P1VE77;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=EII38_01750 {ECO:0000313|EMBL:RRD32484.1};
OS Streptococcus minor.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=229549 {ECO:0000313|EMBL:RRD32484.1, ECO:0000313|Proteomes:UP000281771};
RN [1] {ECO:0000313|EMBL:RRD32484.1, ECO:0000313|Proteomes:UP000281771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH4621_COT-116 {ECO:0000313|EMBL:RRD32484.1,
RC ECO:0000313|Proteomes:UP000281771};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) 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:RRD32484.1}.
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DR EMBL; RQZA01000001; RRD32484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1VE77; -.
DR STRING; 1123309.GCA_000377005_01558; -.
DR Proteomes; UP000281771; 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; cd07431; PHP_PolIIIA; 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 Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR012340; NA-bd_OB-fold.
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 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:RRD32484.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000281771};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RRD32484.1}.
FT DOMAIN 5..70
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1034 AA; 119496 MW; 1F1BF139FA3D4881 CRC64;
MLAQVDTKTV YTFMDSTLTI DKYVARGKEL GYAYLGIMDH NNLYAAYTFM ETCYKAEVRP
LIGCELDLEI QQIPITIQFL ALNSKGYQHL LKISTARMMG QKDFEAIRQY LTDIAIIVPV
ESNQGNLDLG LDYYIGVRPD TPVQRFDRPI LPLYTVRYLK PSDLETLQLL HAIRDNQTLS
QIGWIPAHQE LLSPSQQEAL FKDNFPQAIE NLENLVSDIH YELDKDLKLP RFNRERLAVE
ELQEKAREGL HSKGLLSPQY QERLDKELSI IHKMGFDDYF LIVWDLLRFG RSQGYYMGMG
RGSAVGSLVA YVLEITGIDP VKHDLLFERF LNEERFSMPD IDIDIPDIYR GDFLRYVQKR
YGSMHTAQIV TYSTFGARQA IRDVFKRFGT PEYELTNITK KISFRDSLAS AYERNASFRQ
IINSKPEYQK AYALAKAIEG QPRQTSIHAA GVVMSDNDLT DVIPLKHGED MLITQYDAHA
VEANGLLKMD FLGLRNLTFV QKMKEAVADK YGTQLVIEDI DLEDRKTLEL FAAGKTKGIF
QFEQPGAINL LKRVKPSRFE DLVATTSLNR PGASDYSNNF VKRKHGQERI NLLDDSIADI
LQPTYGIMLY QEQVMQIAQR YAGFTLGKAD LLRRAMSKKD ARQMQHMEEE FLKGAEKLGH
ASENAKAIFA MMAKFAGYGF NRSHAYAYSA LAFQLAYFKT HYPDVFFDIM LNYSSSDYIT
DALQFDFQAA RLTINNIPYH DRFDNKEIFM GLKNIKGFPR EFAFWIVEER PFKSVEDFIL
RLPRQYKKKE LLTPLIQLGL FDIFDKNRHK IISNLENLFV FADAFGSFFA EEEYSWIEAE
DYSDSEKYNL EQSIIGVGIS PHPLLKIRRD ARRPYQELTD LVEGQKVTIL VQIQSIRTIR
TKKTGEQMAF LQVTDTKKKL DVTLFPEIYR RYASDLKEGL IAYLSGRIQE RDGHLQLLLE
NMEKPNVEKF WILLENNQHD GEIALILQDY PGDIPVVLHY QNSNQTIQAQ RMFVKKSEEM
QKRLLGISLK TIFR
//
