ID A0A1M4ZCL0_9LACT Unreviewed; 1119 AA.
AC A0A1M4ZCL0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-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=SAMN02745249_01927 {ECO:0000313|EMBL:SHF15522.1};
OS Atopostipes suicloacalis DSM 15692.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Atopostipes.
OX NCBI_TaxID=1121025 {ECO:0000313|EMBL:SHF15522.1, ECO:0000313|Proteomes:UP000184128};
RN [1] {ECO:0000313|EMBL:SHF15522.1, ECO:0000313|Proteomes:UP000184128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15692 {ECO:0000313|EMBL:SHF15522.1,
RC ECO:0000313|Proteomes:UP000184128};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
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}.
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DR EMBL; FQUF01000037; SHF15522.1; -; Genomic_DNA.
DR RefSeq; WP_073298605.1; NZ_FQUF01000037.1.
DR AlphaFoldDB; A0A1M4ZCL0; -.
DR STRING; 1121025.SAMN02745249_01927; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000184128; 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; cd07431; PHP_PolIIIA; 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 Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR012340; NA-bd_OB-fold.
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:UP000184128};
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 1119 AA; 128158 MW; 632DA65609CE0D52 CRC64;
MSFIQLQVTS THSLMESTLT IQELIKKAKQ EGYEALALTD HNVLYGAIEF YEMALKNNIK
PIIGLTLDVE GFIMKNESYP LLLLAKNFEG YQALIQLSSM YQLNDQNAVP LAEIIVRNEH
LIVISPGDQG EIISLLQNKR IAEAQEVLQY FKENIKDFYL GISLQDSSEE SLSFYKQNRE
NLVALGNVQY LEPKDALPTK ILQVLKSDMP LGSENQARIN QFLSENDRDY SLKSPDEVVQ
QFSAVDLEEA CQATKIIAEN INLKLALNEH IMPTYPVPEG KNSAQYLKAL CDEALEQRVE
EVTEAYVERL EKELKVITTM GFSDYFLIVW DIIRYAHRQK IYTGSGRGSA AGSLVAYLLK
ITNVDPIQYN LLFERFLNEE RYTMPDIDLD FPDNRREEIL TYIYDKYGRK NVAQIGTIGT
YGAKSAVRDV ARVLGASQEE IKRWAKAIPS GPNVSLENGI KNQDLQNLIR ENARNQKIYE
IAKSIEGRNR HISTHAAAVV IADHPVIEQT PLQKGSGSIH LTQYTMEAVE KVGLLKLDIL
GLRNLSILAD CIRFIPYENK GEKIDIDQIP FDDQKTLEIF RKGNTDGVFQ FESAGIRRVL
RKLQPNSFED VVAVNALYRP GPMEQIDTFI RRKNGEEPIK YPHDDLKDIL GITYGVMVYQ
EQVMQVASIM AGYTLNEADI LRRAISKKSH KEIEKGRQQF VQGSIENNYS KETALEVYGY
IERFADYGFN RSHAVAYSKV AYQLAYIKAN YPASFFAAIM KASNKDKIKT YRTESKQYGV
ELLAPDINKS YSSFTVERGK IRFGLDIIKG LPKNFVREII KERRNNGDYV NIVNFLNRID
EKWLNKEIIF PLINSGAFDK LKENRNSLIH SLPSIIDSIK MSHGNVELFD IFAPVIEQKT
EISDEEKMKQ EYEATDFYFT SEPGEKYNEL RKDQTIKYLT DISKDTYVRL LVTVENIKNI
QTKKGQPMSF VDVADSTGKG NLTLFPNVHR QYIQKFDQGD TILIDGKVEQ TKYPAKIIVN
KLALADDLLD EPSKQLEHSN EKKQVLYIRF ESLKSEQKKF YALQEILLQN RGQTPVILYD
QETKEQKPFK QNYNVKVNVQ ILEQLNKMFG EQNIVLKNS
//
