ID A0A1N7EP13_9GAMM Unreviewed; 752 AA.
AC A0A1N7EP13;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=SAMN02745664_10668 {ECO:0000313|EMBL:SIR89843.1};
OS Moraxella cuniculi DSM 21768.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=1122245 {ECO:0000313|EMBL:SIR89843.1, ECO:0000313|Proteomes:UP000187495};
RN [1] {ECO:0000313|Proteomes:UP000187495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21768 {ECO:0000313|Proteomes:UP000187495};
RA Varghese N., Submissions S.;
RL Submitted (JAN-2017) 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; FTNU01000006; SIR89843.1; -; Genomic_DNA.
DR RefSeq; WP_076555154.1; NZ_FTNU01000006.1.
DR AlphaFoldDB; A0A1N7EP13; -.
DR STRING; 34061.B0189_02265; -.
DR Proteomes; UP000187495; Unassembled WGS sequence.
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 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:UP000187495};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 39..180
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 392..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 752 AA; 83137 MW; 982D696B078AABA6 CRC64;
MSTQYQVLAR KYRPKNFHEL LGQTHVAQAL ANAIDTGRLH HAYLFTGTRG VGKTTIARIL
AKCLNCQTGI TSNPCGSCDV CVGIEQGRFL DLIEIDAASR TKVEDTRDLL ENVPYAPAQG
RYKVYLIDEV HMLSTHSFNA LLKTLEEPPA HVKFIFATTD PQKLPITIVS RCLQFVLRPL
SQQLLVEHLA KVLGSEGIDF ANEALWQLAS AAKGSVRDAL SLTDQAIAFG GGMLRSDTVN
QMLGLINQVS IVQLLELIYT DDRRGVAEQI QQMREKMIDA AAVFDELIDS IHQMAVLQVL
PDAPMDTSPE QAAKLQQLSA IIGADTLQLY YEIAIKSREG IRLANTPMQA LEMAILRLLA
FRPLTQAQFV HDDLARAELT DDSDQNDKIA ASVASASPST NETIGNEACD DTDSVDTLDL
QCNDAQSALQ LDEQSINDNQ ADDGDDYQPN HQLINHHDEK SPDNAWQASQ DEPPRMDYPV
SNPALLDDEM MAVSADFVVH DDFADDSAAF QNDTTPPNPA IKDDETTTHD ELEQIDAEPT
LAVLVDNEHE QPKEDFVEKI DDAQKLDANT LAQLDETTHS TDTPSDNKAQ NSTGMVMSQA
QMLDKLKPPS VELVGEWTVQ KWDYWLHLAR TEEIFAADEL ALMANSIMTG QVQGASCLHT
SGDNSQVQAS FASMLEKFAK HYPQIQLADK PVLEEMLAQT PQTLLQSRQL QIREDAQKQL
IDSPVFLHLW QQGFVVNDGT AVLTNSKLSI ET
//
