ID A0A3S9HD58_9LACT Unreviewed; 1111 AA.
AC A0A3S9HD58;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=EJN90_11910 {ECO:0000313|EMBL:AZP05289.1};
OS Jeotgalibaca ciconiae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Jeotgalibaca.
OX NCBI_TaxID=2496265 {ECO:0000313|EMBL:AZP05289.1, ECO:0000313|Proteomes:UP000273326};
RN [1] {ECO:0000313|Proteomes:UP000273326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H21T32 {ECO:0000313|Proteomes:UP000273326};
RA Bae J.-W., Lee S.-Y.;
RT "Complete genome sequencing of Jeotgalibaca sp. H21T32.";
RL Submitted (DEC-2018) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP034465; AZP05289.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S9HD58; -.
DR KEGG; jeh:EJN90_11910; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000273326; 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; 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; SSF50249; Nucleic acid-binding proteins; 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 ECO:0000313|EMBL:AZP05289.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AZP05289.1}.
FT DOMAIN 4..71
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1111 AA; 127449 MW; A40CACE2DAFCDA08 CRC64;
MTFTQLQVIS SYSLLQSTTK LTNLVQSAKE KGYEALALTD YNVLYGQLDF YKLCKKAGIK
PILGIQLELK GNHYQEQTFP IVLLAKNYQG YQKLLKLSTI RSKEDESELK KELQFGLENI
IGITSGEKGE VETLLANNEY EKAKEVVQFW KEIFSVNQFF LGVQLYQKMH PLIEPLQQLS
KEVRVSMIAL NEIRYLNSED QFSCQVLQSI GSNEPIDIHS EEINGEYYLP APEDIYNRYQ
AMGLGELADK TAEVANSIFI ELPLNQPLLP KYPVPEGVSA SEYLKKVCLE GLTMRMKKGK
EDYLERLQYE LSIIHEMGFD DYFLIVWDVM AFAKNASILP GAGRGSAAGS LVAYVLRITH
VDPIEYNLLF ERFLNKERYN MPDIDLDFPD DRRDEVLRYV KDKYGYHHVA QIITFGTLAA
KMSIRDTSRV FGLTPAEASV WSNAIPNQIG IQLKDAYKQS KPLQRLVEKN TTNRLLFETA
MKIEGVPRHI STHAAGVVIS DQPLVELIPL QQRENELSLT QYPMGNVEEI GLLKMDFLGL
KNLSILNDAV QLVEKAEGKA FDIFSIPIND SKTMQLFKES NTNGIFQFES AGIKNVLRKL
GPENLEDLVA VNALYRPGPM EQIDTFISRK KGKQPIDYLH PDLEPILNVT YGVMVYQEQV
MQVASKLAGF TLGEADILRR AIGKKEKATL DREKEHFIQG AINNGYEVKK AEEVYQYIER
FANYGFNRSH SVAYSYIAYQ MAYVKAHYPA AFFAALLNSA NAHSDKMKSY LLDVIKQSVE
LTYPDINQSD WQYSLVNNQI QFGLSGVKGL RRDFISHILV ERKQNGPYQD FVQFLRRIST
KWLKSDLIIP LIASGAFDTF GHTRATLMGS LAGMLSSIEY SGNNVDLIEV LEPRYVEKEE
FPLSELTELE EKYLGYSLLE HPIEEYRHLY KENHIFYIGE LTSKQSTRTM GLIKEVKRIK
TKKGDPMAFL TLTDATGMLN ATLFPEQYVR YIKYLQEGQL VVLTGKYEDK RNENQSSFIV
QKLVLMEEYL LQREKKNQRC FIRMTNEELY DKQFKELISL LKEFPGLCQV VLVDTVRDRK
ILLDEKYRFN PSKESVEKLN RLFGEKNVVI Q
//
