ID A0A1R1BWC6_9BACL Unreviewed; 1207 AA.
AC A0A1R1BWC6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=BK127_19575 {ECO:0000313|EMBL:OMF14129.1};
OS Paenibacillus sp. FSL H7-0331.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1920421 {ECO:0000313|EMBL:OMF14129.1, ECO:0000313|Proteomes:UP000187480};
RN [1] {ECO:0000313|EMBL:OMF14129.1, ECO:0000313|Proteomes:UP000187480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H7-0331 {ECO:0000313|EMBL:OMF14129.1,
RC ECO:0000313|Proteomes:UP000187480};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (NOV-2016) 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:OMF14129.1}.
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DR EMBL; MRTH01000012; OMF14129.1; -; Genomic_DNA.
DR RefSeq; WP_076233174.1; NZ_MRTH01000012.1.
DR AlphaFoldDB; A0A1R1BWC6; -.
DR STRING; 1920421.BK127_19575; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000187480; 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; 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:UP000187480};
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 1086..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1207 AA; 135870 MW; 55025C8B6BBEF689 CRC64;
MSDFVHLHVH SEYSLLDGAA RIDDMVGQAA AMGMKSLALT DHGVMYGAIP FYKACKRHGI
KPIIGCEMYY TAGSIRDKGT RKEHPIYHLI LLAKNQVGYQ NLMKLCSIGH LQGHHYKPRI
DPQHLAQYSE GLICTSSCLG GEVSQHLLHE RYEQAKEAAL RYRAIFGDDF FLELQDHGLL
EQKKVNQSML RLSEDTGIPL VATNDVHYVR EPDHAVQDIL LCIGTGKTVD DPDRLKFQSS
QLYLKSAEEM NRLFPHVLQA IANTSIIAER CQLEIEFGRS ILPRFEPIPD HSTAGEYLAE
LCRVGLRTRY EHSDSWQDPS FCKQIEERLV YELSVIERMG FSDYFLIVWD FIRFAHEQRI
ATGPGRGSSA GSLVAYVLRI TDVDPIRYKL LFERFLNPER ISMPDIDIDF SDLRRDEVID
YVVAKYGPEH VAQIITFGTM AAKAAVRDVG RVLNLPYNEV DRAAKMIPHQ LGMTLAEAVE
ANPDLKALAA RQPKTAELLD MAMKVEGMPR HASTHAAGVV ISREPLTQYV PLQEGNEQTA
LTQYSMEHLE AIGLLKMDFL GLRTLSIIER TLMWIKEQTG IELDFHKLSI DDPATYEMLG
RGDTTGVFQM ESPGVRKVLK ELRPSGFEDI ISVVALYRPG PMEFIPRFIQ GKHGEIEVEY
PHVDLEPILR DTYGIIVYQE QIMQIASQMA GFSLGEADLL RRAVSKKKRE VLDEERAHFV
KGSQSLGYSA AEANKVYDMI VRFADYGFPR AHATAYGVLA FQTAYLKAHY PVQFMASMLT
AVMGNHNKVA EYVDECRRMG IAVLPPDVNE SGIVFTPAKQ PQSLEESEDN PVSFGAIRFG
LAAIKNVGTH AIETIMQERS SDEGSFESLI DLCRRVDLRV CNKRVLESLI QGGAAGSLPG
HRAQQLAMLE DTINAALKWR KERDDLQLHL FGFVEDVNWD VEYPQIAPYT MTQQLEFEKE
LLGLYISGSP LDDYEQVLRE LEIDLLHYLP EMPDHSEVIV AGLVLSSKTI VTKKGQPMAF
MELEDRVSKV EVVLFPEVWK QYAPLVQKGK PVLIKAKLQQ GDEEVKLLAD QLFALNDPEL
LANAMRRPAA PTHKPGSRTV SKPDKGKSTN ERTVTPPAAR EVQPNKAVSP PSNQRVYIKI
SPAHERQRIL SSLKELLLQH QGSLSVVLYY ESSQKTLSLN DQFNVKPSPK LIQVIEDLLG
KDTARVK
//
