ID A0A0R2CH59_9LACO Unreviewed; 1115 AA.
AC A0A0R2CH59;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=FC80_GL001005 {ECO:0000313|EMBL:KRM91009.1};
OS Liquorilactobacillus cacaonum DSM 21116.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423729 {ECO:0000313|EMBL:KRM91009.1, ECO:0000313|Proteomes:UP000051131};
RN [1] {ECO:0000313|EMBL:KRM91009.1, ECO:0000313|Proteomes:UP000051131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21116 {ECO:0000313|EMBL:KRM91009.1,
RC ECO:0000313|Proteomes:UP000051131};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRM91009.1}.
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DR EMBL; AYZE01000014; KRM91009.1; -; Genomic_DNA.
DR RefSeq; WP_057829218.1; NZ_AYZE01000014.1.
DR AlphaFoldDB; A0A0R2CH59; -.
DR STRING; 1423729.FC80_GL001005; -.
DR PATRIC; fig|1423729.3.peg.1018; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000051131; 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 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 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.
PE 4: Predicted;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000313|EMBL:KRM91009.1};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000051131};
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 1115 AA; 126634 MW; C316D55064B6E463 CRC64;
MGGAALQVIS SYSLLQSSIR IEEVVLNAKQ RGYTALALAD INVLYGALSF YDACMANGIK
PLIGMTLETS TQNKETLVVI AKNEVGYRNL MQISTKKQLL LAKNILDFSI EENINLFEDL
IIIIPPNNSF FANKILDGKV DIAKKYLSFL YNIIGEDLYV GVNTTLDETF YETILQYANF
VGVETIAFDT IKYLEKNGKF ICEVLEAIKR GETLDYKKLQ YANKSKGINW LKPVSSLEAS
YVEVNRAKAF QNMLSLIEQF DFKLESKRIT LPKYKTPNGY DANTYLKKLC DEGLQKKFSK
QSENDKANYL DRMNKELLTI EKMRFADYFL IVWDVTNYAR ENQILVGPGR GSAAGSLISY
LLGITEVDPL KYNLFFERFL NEKRAQMPDI DLDIPDNRRQ EIIEYVNRRY TEGHMAQIIT
FGTFGAKQAL RDVARVMGIS QVESDNWSRL IPSGPGINLR KAQQSSAKLQ THINKNEQNQ
LLFRTAMLLE GLPRHYSVHA AGIVLSDTDL KQVVPLQMGN ENILLTQYTK NDVERVGLLK
IDFLGLRNLT ILNNTLLSIK RNFNKSVDIN QIPLDDRKTL NLFQQAETSG VFQFESGGIR
NVLRKLHPTS FEDIAAVNAL FRPGPMENID SFIARKHGRE KITYPNDSLI PILKNTYGIL
VYQEQVMQVA SVMGGFSLGQ ADMLRRAMSK KNAAVIKDLK SKFVKGALAL GYSNETAKKV
YDYIAQFANY GFNRSHAVAY SKMAFQLAFL KVHYPASFFG ALLNAVMGDI KKTREFLLEA
KQYGLLLKSP SINKSNYYTI SGKNELLIGL GNIKTLRRDF IKSIITERKI GGWYKSFNDF
LSRIDHKYLK VDPIKALIYS GAFDSFSENR ATLLGNLEKN ISNVELSGEN SELLSLLAPK
SKKFDELSLD ELLAGEKKYL GLFLSAHPVE KFDKVAKFYN TNLIAKTRAN TNPRILCLIK
EIKVIRTKTG EQMAFITVED QSGEIDLTLF PRVFDRVTED LELNKVYLVD GKSEIRHQKM
QLIVSRMNLA EKLKIEMKEK LFLRLPSESS SSEKENLLNI LQSNAGNIPV VLYEEKTAIK
WVLDKKYWVN KSSEVKKQLD NLIGKNNVVF RNESK
//
