ID A0A1S2R0K8_9BACI Unreviewed; 1119 AA.
AC A0A1S2R0K8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-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=BIV59_13065 {ECO:0000313|EMBL:OIK11145.1};
OS Bacillus sp. MUM 13.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1678001 {ECO:0000313|EMBL:OIK11145.1, ECO:0000313|Proteomes:UP000180199};
RN [1] {ECO:0000313|EMBL:OIK11145.1, ECO:0000313|Proteomes:UP000180199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUM 13 {ECO:0000313|EMBL:OIK11145.1,
RC ECO:0000313|Proteomes:UP000180199};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Bacillus sp. MUM 13.";
RL Submitted (OCT-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:OIK11145.1}.
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DR EMBL; MLYQ01000044; OIK11145.1; -; Genomic_DNA.
DR RefSeq; WP_071351942.1; NZ_MLYQ01000044.1.
DR AlphaFoldDB; A0A1S2R0K8; -.
DR Proteomes; UP000180199; 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 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:UP000180199};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..70
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1119 AA; 126247 MW; BD8019DA5C63F738 CRC64;
MFVPLHIQSA YSLLTSTVRI KELAALAKEQ GYKALALTDR NVMYGSLYFY KECKKLGIKP
IIGLLADILD DAEESFPMIL LAENNDGYQN LLKISSAIKT KSPKGLPHKW LKAYSRGLIA
ISPGAEGKIE NLLAENQEEK AYEAAGLFAD IFGPRRFFLS IQRQSPDAKS EMEAKIGKLA
ANQGLDIIAT NPAFYLMKED AMSQEVLLAI KNGAKLSEED RERLPSNEFY LKDPRKMAEL
FQDCPEVLEN TLKIAARCQV DIAFNRPLLP QYPAEPGVSS DELLKIICEK GLEKRRPQAP
HSYMERLHYE LDIIKKMNFS DYFLIVWDFM KFARQKGILT GPGRGSAAGS MVAYVLSITE
VDPIEHHLLF ERFLNPERVS MPDIDIDFPD NRREEVISYV ASRYGEFHVA QIITFGTLAA
KAALRDTGRV FGLNPKEQET ISKMIPGRIG ISLEDALRES KALREFVNQS ELNKRLFDTA
SKLEGLPRHT STHAAGVVIS GQPLTDLIAI QEGHAGIHLT QFPMDLLEEL GLLKMDFLGL
RNLTLIDLII SAVQKDTGQK IDIASLPLKD EKTFRLLSKG ETTGVFQFES DGIRNVLKRL
NPTDFEDIVA VNALYRPGPM ENIPLFIQRK HGMAEETYPI PELKEILKDT YGVIVYQEQI
MQIASAMAGF TLGQADLLRR AVSKKKKDIL DQERQHFIKG ALMQGYEEHA ASEIYDLIVK
FSNYGFNRSH AVAYSMIAYQ LAYLKAHYPS YFMAALMTSV IGNEDKISQY VRESRKMGIQ
VLPPSINSSG FPFKADKESI LFSLGPIKGI GGAVLKEIFS ARRQKKFEDL FDFCLRVSGK
AVNRKILEAL VHSGAFDEFG KDRATLLASL DVALSHSELV NPDDSQFDFF ESSEFSLKPK
YIEVDPIRLE DKLYYEKNAL GFYLSNHPVT GYRNVFSHFG AVSIDEAIIS KEPKIFLGVY
ITSVKTIRTK KGEVMAFLSV GDENGDLEAV AFPNVYSKHS SILSNGEILM IQGTMEERDG
KKQLIIHDAY MLEKLYRMME EDKTRLFIKI EQDKQTNPIL QKIKQALLKH SGTTQVMLYY
ESEERYVQLS LRDWVTPSRE LLARLETIAG EGNVILQQE
//
