ID A0A0R1YIH8_9LACO Unreviewed; 583 AA.
AC A0A0R1YIH8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA polymerase III subunit gamma/tau {ECO:0000256|RuleBase:RU364063};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU364063};
GN Name=dnaX {ECO:0000256|RuleBase:RU364063};
GN ORFNames=FD40_GL000898 {ECO:0000313|EMBL:KRM42114.1}, LA20533_01815
GN {ECO:0000313|EMBL:APT18094.1};
OS Amylolactobacillus amylophilus DSM 20533 = JCM 1125.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Amylolactobacillus.
OX NCBI_TaxID=1423721 {ECO:0000313|EMBL:KRM42114.1, ECO:0000313|Proteomes:UP000051230};
RN [1] {ECO:0000313|EMBL:KRM42114.1, ECO:0000313|Proteomes:UP000051230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20533 {ECO:0000313|EMBL:KRM42114.1,
RC ECO:0000313|Proteomes:UP000051230};
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).
RN [2] {ECO:0000313|EMBL:APT18094.1, ECO:0000313|Proteomes:UP000185499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20533 {ECO:0000313|EMBL:APT18094.1,
RC ECO:0000313|Proteomes:UP000185499};
RA Lee Y.-J., Yi H., Bahn Y.-S., Kim J.F., Lee D.-W.;
RT "The whole genome sequencing and assembly of Lactobacillus amylophilus DSM
RT 20533T strain.";
RL Submitted (DEC-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.
CC {ECO:0000256|RuleBase:RU364063}.
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 ECO:0000256|RuleBase:RU364063};
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|RuleBase:RU364063}.
CC -!- SIMILARITY: Belongs to the DnaX/STICHEL family.
CC {ECO:0000256|ARBA:ARBA00006360, ECO:0000256|RuleBase:RU364063}.
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DR EMBL; CP018888; APT18094.1; -; Genomic_DNA.
DR EMBL; AYYS01000013; KRM42114.1; -; Genomic_DNA.
DR RefSeq; WP_056946492.1; NZ_CP018888.1.
DR AlphaFoldDB; A0A0R1YIH8; -.
DR STRING; 1423721.LA20533_01815; -.
DR KEGG; lah:LA20533_01815; -.
DR PATRIC; fig|1423721.4.peg.912; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000051230; Unassembled WGS sequence.
DR Proteomes; UP000185499; Chromosome.
DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR CDD; cd18137; HLD_clamp_pol_III_gamma_tau; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR022754; DNA_pol_III_gamma-3.
DR InterPro; IPR012763; DNA_pol_III_sug/sutau_N.
DR InterPro; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR02397; dnaX_nterm; 1.
DR PANTHER; PTHR11669:SF0; PROTEIN STICHEL; 1.
DR PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR Pfam; PF13177; DNA_pol3_delta2; 1.
DR Pfam; PF12169; DNA_pol3_gamma3; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU364063};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA replication {ECO:0000256|RuleBase:RU364063};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU364063};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364063};
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU364063};
KW Reference proteome {ECO:0000313|Proteomes:UP000051230};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 540..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 368..395
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 583 AA; 64832 MW; 1CB450807AE1EA6E CRC64;
MAYQALYRKW RPRTFADVIG QESITSTLRN SIRINKISHA FLFAGPRGTG KTSCAKILAK
TVNCLNIKDG EPCNECANCL AADENRMSDL IEIDAASNNG VDEIRDIRDK VKYAPTEGKY
KVYIIDEVHM LSMGAFNALL KTLEEPPEHV IFILATTELQ KVPATIISRT QKYTFKRIAL
DAIIARLKQI LVAEEISYED KALQVIAQVA DGGMRDALSI LDQIISFEKD GVTYADALEI
TGFANQEKIE ELFLLLTQQE TGAALALNKE LLAAGINPQN ILNELVELAT QVLISQKTKT
KSSAFLTNEL SETVESLDNR AILYLIDTAN EALNDLRFTT QQNVPLDIFC VKVTSFHPAG
DEQQSGRQTD TSEEMQELQK QVQHLSQQLG ALQKTGVVPR MKSATTTGAS VKSTVASTNL
KTKYRASVYH VLKHATKDDL SRVKDVWPDL ISKLEVSQRA MMKVSKPVAA GPDACVVAFD
YQLWFERATS DSELMKQLND GLTSLTHANT EIVLVPKNEW PILRADYLKT HKAELTNRQE
VDETETAAQA DEADNSQSKD VVKNDIIEQA RQLFGDDMID VKD
//
