ID R4K5C0_CLOPA Unreviewed; 1167 AA.
AC R4K5C0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=Clopa_3575 {ECO:0000313|EMBL:AGK98357.1};
OS Clostridium pasteurianum BC1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=86416 {ECO:0000313|EMBL:AGK98357.1, ECO:0000313|Proteomes:UP000013523};
RN [1] {ECO:0000313|EMBL:AGK98357.1, ECO:0000313|Proteomes:UP000013523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC1 {ECO:0000313|EMBL:AGK98357.1,
RC ECO:0000313|Proteomes:UP000013523};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Dunn J.,
RA Taghavi S., Francis A., van der Lelie D., Woyke T.;
RT "Complete sequence of chromosome of Clostridium pasteurianum BC1.";
RL Submitted (JAN-2012) 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}.
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DR EMBL; CP003261; AGK98357.1; -; Genomic_DNA.
DR RefSeq; WP_015616640.1; NC_021182.1.
DR AlphaFoldDB; R4K5C0; -.
DR STRING; 86416.Clopa_3575; -.
DR KEGG; cpas:Clopa_3575; -.
DR PATRIC; fig|86416.3.peg.3573; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_9; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000013523; 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 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 ECO:0000313|EMBL:AGK98357.1};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000013523};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..78
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1167 AA; 134291 MW; 71C8D606AE2C4D4A CRC64;
MEKESSYEDF VHLHVHTEYS LLDGSGKIGK LISRAKELGM KSLAITDHGA MYGVVDFYKA
AKEKGIKPII GCEVYVAGKS MHIKRPDKEN ETYHLVLLVK NDEGYKNLMQ IVSSASIEGF
YYKPRVDHDF LRQHSKGIIA LSACLGGEVQ SKILKNNKEK AKEAALFYKE IFKDGFYLEL
QYHGIDEQLR VNEELVNMSR ELEIPLVATN DVHYINREDY KSHDVLLCIQ TGKTVDEENR
MRYASDEFYL KSPEEMYNQF SYVQEALENT CKIAEECNFD YEFHKSKLPN FPLDEGIDHF
EYMKELCYDG LKKRYNPITE KLTQRLEYEL GIIREMGYVD YFLIVWDFIR FARENGIMTG
PGRGSGAGSI VAYTLGITKI DPIEYNLIFE RFLNPERVSM PDIDSDFCYE RRQEVIDYVV
EKYGKNNVSQ IVTFGTMAAR ACIRDVGRAM NYSYAEVDRI AKMIPSMLNI TIDKALEINQ
ELKQIYDEDE KVKALIDVAR DLEGLPRHTS THAAGVVIAS QPLVNYVPLL RNEEAIVSQF
TMGTLEELGL LKMDFLGLRT LTVLRDAINM IRDNKGIKID LDAIDFNDKK VYKMLGEGKT
VGVFQLESPG MTSFMKELKP DNLEDIIAGI SLYRPGPMNE IPRYIKNKNN PEKVEYITPE
LEPILNVTYG CMVYQEQVMQ IVRDLAGYSM GRSDLVRRAM SKKKHHVMEQ ERHNFIHGIA
AEDGTVEVEG CLRRGISEEA ANKIFDSMMD FASYAFNKSH AAAYAVVAYE TAYLMKYYPT
EFIAAMLNSV MGNNEKVAYY VRFAKEINIE LLPPDINESF SRFTVKGDKI RFGMAAVKNV
GVNVVESVVN SRKEKGTFNS LVDFCNKVDI GEVNKRAVES LIKVGAFDYF KIYRSRLLAV
YEKVMDGISN QKKKNIDGQI SLFSNFQKDD ESSYRDMEIK YPDIKEFEKK YILSMEKEMT
GLYISGHPLD EYKETLDISV NTKISDIIVE ESLDEVEDSE NYKVRDGDRV IIGGILTEVT
RKITKNNSMM AFFKIEDMYA AIEVIIFPKV LEKFNMLIKE DEMLIIKGRV SIREEEQPKI
LCEDIKPLVK INNSKVYIQI EQENQVVNTI KEIEIFLSEF KGSTPIYICT KKERKKFMLP
KDLWINEDTE VLDFLRKRFG EENLKVC
//
