ID A0A369B9R1_9BACL Unreviewed; 1248 AA.
AC A0A369B9R1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=DFP94_10919 {ECO:0000313|EMBL:RCX17296.1};
OS Fontibacillus phaseoli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Fontibacillus.
OX NCBI_TaxID=1416533 {ECO:0000313|EMBL:RCX17296.1, ECO:0000313|Proteomes:UP000253090};
RN [1] {ECO:0000313|EMBL:RCX17296.1, ECO:0000313|Proteomes:UP000253090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8333 {ECO:0000313|EMBL:RCX17296.1,
RC ECO:0000313|Proteomes:UP000253090};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUL-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:RCX17296.1}.
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DR EMBL; QPJW01000009; RCX17296.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369B9R1; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000253090; 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; cd12113; PHP_PolIIIA_DnaE3; 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 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; SSF160975; AF1531-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000253090};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..72
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 834..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1248 AA; 138033 MW; EF214C9037C46F44 CRC64;
MDSFVHLHVH SEYSLLDGAA RLEDLVATAA GFGMKSLALT DHGVMYGAVP FYKLCKAHGI
KPIIGCEMYF TAASRKERGS RKDQPIHHLI LLAKNETGYR NLMRLCSIGH LEGFHYKPRI
DWEVLERHKE GLICLSACLG GEVPQHLLHG RLEEAKRAAL RYREAFGEDF YLELQDHGIP
EQKKVNPLLV DLARETGIPL VATNDVHYLG HDDAEVQDVL ICIGTGKTVD DEDRFKINTS
QLYLKSGEQM AELFPHLPEA IANTDLIAEK CQLELEFGRH ILPAYRPIPE GMTPGAYLAY
LCERGLNERY GHLEEWQGEA QKAKLKERLG YELTVIGNMG FSDYFLIVWD FIAYAHRNGI
ATGPGRGSSA GSLVAYVLRI TDVDPMKYKL LFERFLNPER ITMPDIDIDF SDERRDEVIA
YVAEKYGPEH VAQIITFGTM AARAAVRDVG RALNVPFGEV DKVAKLIPGF IGMTIERALK
ESPDLKQMYD SHARIKGLLD MAKKVEGMPR HASTHAAGVV ISRDPLTDAV PLQAGSEGTA
LTQYSMENLE SVGLLKMDFL GLRTLSIIER CMRWIGEQTG KAPDFRMIAD DDPMTYDMLG
HGETTGVFQL ESAGCRRVLR DLKPSVFEDV ISVVALYRPG PMEFIPKFIS SKHGETKVEY
PHPDLEPILK DTYGIIVYQE QIMQIASVMA GFSLGEADLL RRAVSKKKRE VLDEEREHFV
TGSIALGYRE EEANAVYDMI VRFANYGFPR AHAAAYGVLA FQTAYLKAHY PVHFMASMLT
AVMGSHRKVA EYIVECRRMG ITVLPPDVNE SGVLFTPQAK AGLGLSVPSG EGVMQDDGYG
HHSGNIDTSD NSATSGDPAL SDHLDASPGV IRFGLAAIKN VGTQAMESIL QERKESPFDS
LLDFCRRVDL RVCNKRVIES LIQGGAFDGL PGHRAQLLAM LDETVEAAMK WRKEREDLQI
QLFDFVETPN WNIEYPEIQK FTVTQQLELE RELLGLYLSG HPLDDFDEQL EQSGIDRLMD
LAEAPDESKA IVAGMVVSVK AITTKQGKAM AFMELEDQIE RCEVVLFPEV WRRCSPHIAK
GALLALRATV QQQDEGFKLL ADEVAPLSAQ SLAQLKRGLA SRSGRAAAGS PPGAAKGARS
GSASAAPPAT AAAQTRPAAV AGAPAGRERK TPAEQRVFIK ITAAAESAGL LEKLKAVLEL
HPGPVPTVLF YESTGKLLAL NERYRIKPSP DLFRELEQLL GPDTVKVK
//
