DPO3A_STAAM
ID DPO3A_STAAM Reviewed; 1065 AA.
AC P63979; Q99TG0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=DNA polymerase III subunit alpha;
DE EC=2.7.7.7;
GN Name=dnaE; OrderedLocusNames=SAV1703;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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 (By similarity). {ECO:0000250}.
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 -!- 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 complex
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC subfamily. {ECO:0000305}.
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DR EMBL; BA000017; BAB57865.1; -; Genomic_DNA.
DR RefSeq; WP_000226919.1; NC_002758.2.
DR AlphaFoldDB; P63979; -.
DR SMR; P63979; -.
DR World-2DPAGE; 0002:P63979; -.
DR PaxDb; P63979; -.
DR EnsemblBacteria; BAB57865; BAB57865; SAV1703.
DR KEGG; sav:SAV1703; -.
DR HOGENOM; CLU_001600_0_0_9; -.
DR OMA; NECRRMG; -.
DR PhylomeDB; P63979; -.
DR BioCyc; SAUR158878:SAV_RS09135-MON; -.
DR Proteomes; UP000002481; 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 Gene3D; 1.10.10.1600; -; 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; 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 InterPro; IPR004805; PolC_alpha.
DR PANTHER; PTHR32294; PTHR32294; 2.
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; SSF89550; 1.
DR TIGRFAMs; TIGR00594; polc; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA replication; DNA-directed DNA polymerase;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..1065
FT /note="DNA polymerase III subunit alpha"
FT /id="PRO_0000103340"
SQ SEQUENCE 1065 AA; 122836 MW; EB23C016E20AB196 CRC64;
MVAYLNIHTA YDLLNSSLKI EDAVRLAVSE NVDALAITDT NVLYGFPKFY DACIANNIKP
IFGMTIYVTN GLNTVETVVL AKNNDGLKDL YQLSSEIKMN SMENVSFELL QQFSSNLIII
FKNVADEHRD IVQVFDSHED TYLDHQSVLV QGIKHVWIQN VCYQTRQDAD TISALAAIRD
NAKLDLIHDQ EDFGAHFLTE KEIKQLDINQ EYLTQVDVIA QKCNAELKYH QSLLPQYQTP
NDESAKKYLW RVLVTQLKKL ELNYDVYLER LKYEYKVITN MGFEDYFLIV SDLIHYAKTN
DVMVGPGRGS SAGSLVSYLL GITTIDPIKF NLLFERFLNP ERVTMPDIDI DFEDTRRERV
IQYVQEKYGE LHVSGIVTFG HLLARAVARD VGRIMGFDEV TLNEISSLIP HKLGITLDEA
YQIDDFKKFV HRNHRHERWF SICKKLEGLP RHTSTHAAGI IINDHPLYEY APLTKGDTGL
LTQWTMTEAE RIGLLKIDFL GLRNLSIIHQ ILIQVKKDLG INIDIEKIPF DDQKVFELLS
QGDTTGIFQL ESDGVRSVLK KLKPEHFEDI VAVTSLYRPG PMEEIPTYIT RRHDPSKVQY
LHPHLEPILK NTYGVIIYQE QIMQIASTFA NFSYGEADIL RRAMSKKNRA VLESERQHFI
EGAKQNGYHE DISKQIFDLI LKFADYGFPR AHAVSYSKIA YIMSFLKVHY PNYFYANILS
NVIGSEKKTA QMIEEAKKQG ITILPPNINE SHWFYKPSQE GIYLSIGTIK GVGYQSVKVI
VDERYQNGKF KDFFDFARRI PKRVKTRKLL EALILVGAFD AFGKTRSTLL QAIDQVLDGD
LNIEQDGFLF DILTPKQMYE DKEELPDALI SQYEKEYLGF YVSQHPVDKK FVAKQYLTIF
KLSNAQNYKP ILVQFDKVKQ IRTKNGQNMA FVTLNDGIET LDGVIFPNQF KKYEELLSHN
DLFIVSGKFD HRKQQRQLII NEIQTLATFE EQKLAFAKQI IIRNKSQIDM FEEMIKATKE
NANDVVLSFY DETIKQMTTL GYINQKDSMF NNFIQSFNPS DIRLI