ID A0A0Q5UE54_9SPHN Unreviewed; 1166 AA.
AC A0A0Q5UE54;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=ASG20_17795 {ECO:0000313|EMBL:KQS47077.1};
OS Sphingomonas sp. Leaf198.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736299 {ECO:0000313|EMBL:KQS47077.1, ECO:0000313|Proteomes:UP000050871};
RN [1] {ECO:0000313|Proteomes:UP000050871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf198 {ECO:0000313|Proteomes:UP000050871};
RA Garrido-Oter R.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000050871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf198 {ECO:0000313|Proteomes:UP000050871};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQS47077.1}.
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DR EMBL; LMPX01000004; KQS47077.1; -; Genomic_DNA.
DR RefSeq; WP_056055926.1; NZ_LMPX01000004.1.
DR AlphaFoldDB; A0A0Q5UE54; -.
DR STRING; 1736299.ASG20_17795; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000050871; Unassembled WGS sequence.
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 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; 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 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:UP000050871};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..73
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1166 AA; 127639 MW; F2F727304D913AF3 CRC64;
MHSGYVPLRV FSCYTMLDGA IDPKAIAKQA RALGFPAAAL TDRNGLYAAM AYSDAAKKDG
VQPIIGVMLG VGRPDMPDGV ATQFDWLALY AQNMTGYDNL CALVSMAHLD RPIEMPAHVD
FAALERHTDG LIALTAGGEG GLARLFAEGQ PDRARAYLDR LQGLFDDRLY IELSRRNDAI
ETAAEADLID IAYERNLPLV ATNPCCFTES AFGDAHDAML CIAHSTYVET EDRIRSCPEA
WMKPAKVMHE MFADLPEAIA NTLVVAQRCA VMAPYRKPIL PSLAGDIEGE AKLLRDDAEA
GLEARLARIT ELHGEGEDGW RDVYRKRLAF EVDVIVQMGF PGYFLIVADF IKWAKDHDIP
VGPGRGSGAG SVVAWSLTIT DLDPIKLGLL FERFLNPERV SMPDFDIDFC ETRRVEVIRY
VQEKYGRDQV AQIITFGKLK ARAVLKDTGR VLQMSYGQID RLAKLVPNHP TDPWTLERAL
NGVGELAKEY ANDNGVRKLL DLAMKLEGLP RHSSTHAAGV VIGDRPLAQL VPLYRDPRSD
MPVTQFDMKY VEGAGLVKFD FLGLKTLSVL QKAVQLLAKR GVTVDLEALE WDDAGVYALL
QKGDTVGVFQ LESEGMRRTL SAVRPSNFGD IIALVSLYRP GPMDNIPSFG RRKNGTEAID
YPHPLLEPIL SETYGIFVYQ EQVMQAAQVL AGFSLGGADL LRRAMGKKVK AEMDAQRAGF
VEGCLTVNGI KKAEANALFD LIDKFAGYGF NKSHAAAYAL LAYQTAWLKA HHPHEFFAAS
MCYDLHQTDK LAIFTDDMRR LGITALPPCI NASQAEFDVE VLPDVEENNL AVRYALGALK
SVGEGAMEKL IVERVQNGPF AGLDDLAKRV DPRLLNKRQL ETLAAAGAFD GLDQNRAGIH
ATAETILAIA ARTHEQKTSG QGGLFGDAEP AGDAIKLPPS VRWTLSQRMD QEKEAFGFYF
SAHPVDRHRH IAVSHGARAY TALSELNIPD DGSRAGATMA VLVEDARYRT SARGKRFMMA
QCSDASGQFM ATCFDDQVSR DLEEAAKAGG CGLITVELDR KPGEDTPRVS IKRIQPFEGL
ANLARFQVVV TISDMSAFAG LASLLAEHRG ARGEVRVRAP TPDGEVCILL GRDFLLDGEL
VEHIESLHGV AKVEMKTSET RLALVG
//
