ID A0A221MBJ4_9BACI Unreviewed; 1117 AA.
AC A0A221MBJ4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=CFK40_08295 {ECO:0000313|EMBL:ASN05011.1};
OS Virgibacillus necropolis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=163877 {ECO:0000313|EMBL:ASN05011.1, ECO:0000313|Proteomes:UP000204391};
RN [1] {ECO:0000313|EMBL:ASN05011.1, ECO:0000313|Proteomes:UP000204391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 19488 {ECO:0000313|EMBL:ASN05011.1,
RC ECO:0000313|Proteomes:UP000204391};
RX PubMed=12710619; DOI=10.1099/ijs.0.02371-0;
RA Heyrman J., Logan N.A., Busse H.J., Balcaen A., Lebbe L.,
RA Rodriguez-Diaz M., Swings J., De Vos P.;
RT "Virgibacillus carmonensis sp. nov., Virgibacillus necropolis sp. nov. and
RT Virgibacillus picturae sp. nov., three novel species isolated from
RT deteriorated mural paintings, transfer of the species of the genus
RT salibacillus to Virgibacillus, as Virgibacillus marismortui comb. nov. and
RT Virgibacillus salexigens comb. nov., and emended description of the genus
RT Virgibacillus.";
RL Int. J. Syst. Evol. Microbiol. 53:501-511(2003).
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}.
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DR EMBL; CP022437; ASN05011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221MBJ4; -.
DR KEGG; vne:CFK40_08295; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000204391; Chromosome.
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:UP000204391};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..71
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1117 AA; 127837 MW; 85E1C87231E50266 CRC64;
MSFTHLQVKS GYSLMESTIT IDKLVKKAAD LNFQALALTD DHVLYGAIPF YKACKSHGIK
PIIGINVQVI DEHTEEITCI LLAKNNQGYK QLMKLSTDVQ LSDNKNIEFA QLNKYTQDLI
GIVSTTSKEI GIRFENQSFE EINEYLAHWK QAFAGGDFYL SVEDHGKERD KTLHQKVQTY
SIRERVNVVA VNDVRYLDQK DDHAYDCLQA IKKGQQWVPT NNPSVPHHHL RSSDEMDSLF
GLTWPEVIEA TNGIVEKCNV ELNFDERLLP SFAVPEEMDA HTYLEKQCFD NLETKFKSVS
NEVKERLKYE LSVIKSMGFS DYFLIVWDFI NYAKRNDIVV GPGRGSAAGS LVAYVLSITD
VDPIKHQLLF ERFLNPERIT MPDIDIDFSD NRRDEVIDYV RDKYGVDHVA QIITFGTFAA
RSLVRELIKT IGIDQQDAYF LLKEIPIQAN KSLLDYIQAS EDLKKYIKQS ASLKALFTIA
LKLEGLPRHV STHAAGVVIS EKPLVEHIPL TIGSSHTLLT QYPMNELESV GLLKMDFLGL
RNLTLLERVI KSIGQTQNKQ LHLDEIPESD EETFNLLQSG MTDGIFQLES EGMKQVLTKL
KPTSFEDIVA VNALYRPGPM ENIPTYISRK HNQSPIHYPH PDLEPILKKT YGVLIYQEQI
MQIASHLAGF SLGKADILRR AVSKKQHELM DEQRETFIAG CLNNGYDEAV AIEIFDWIVQ
FSNYGFNRSH AVAYSKISYQ LAYLKAHYPA SFFAELLSTS VNQQEKVHHY RKEAKDFKLE
FLPPNINNSF GKYTVEHGQI RMGLLSIKGI GNQAVKEIVR ARKSGPFKSI FDFCLRISTK
LINRQSMELL IMVGAFDDTY HNRASLLATI DHAMEQGELF REFADQPSLF QDKMDLEVTY
VEIEDFSLMK KLADEKELVG IYISSHPLAS YREKLRMSGY LTLNQANRMV GKRNVKSAVI
IQSMKTIRTK RGDPMAFVTI GDETSEMEAV IFPDVFREVN RWLNEEVIIL ITGKIELRNN
KNQWLVQEIH QFNEEDVKAK ANQRLFVKFS EQNSEKVLLN MKEIAINHPG NTPVIIHRED
KKQTYQLASE YFMEATRECL QELKGYFGEA NVVLKKE
//
