ID A0A1I3VRB4_9RHOB Unreviewed; 587 AA.
AC A0A1I3VRB4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN04488138_11736 {ECO:0000313|EMBL:SFJ97928.1};
OS Celeribacter halophilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=576117 {ECO:0000313|EMBL:SFJ97928.1, ECO:0000313|Proteomes:UP000183299};
RN [1] {ECO:0000313|EMBL:SFJ97928.1, ECO:0000313|Proteomes:UP000183299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8891 {ECO:0000313|EMBL:SFJ97928.1,
RC ECO:0000313|Proteomes:UP000183299};
RA de Groot N.N.;
RL Submitted (OCT-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; FORY01000017; SFJ97928.1; -; Genomic_DNA.
DR RefSeq; WP_066602357.1; NZ_QKZJ01000019.1.
DR AlphaFoldDB; A0A1I3VRB4; -.
DR STRING; 576117.SAMN04488138_11736; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000183299; 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; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR022754; DNA_pol_III_gamma-3.
DR InterPro; IPR022107; DNA_pol_III_gamma/tau_C.
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 Pfam; PF12362; DUF3646; 1.
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:UP000183299};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 42..189
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 382..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 63630 MW; F041153D224C2BCE CRC64;
MTDTNSGYKV LARKYRPETF ADLIGQDAMV RTLKNAFAAD RIAQAFIMTG IRGTGKTTTA
RIIAKGMNCI GPDGNSGPTT EPCGQCEHCV AISEGRHVDV MEMDAASRTG VNDIREIIDS
VHYRAASARY KIYIIDEVHM LSTSAFNALL KTLEEPPAHV KFIFATTEIR KVPVTVLSRC
QRFDLRRIEP EVMMNHLASI AEKEGSKVAQ DAFALITRAA EGSVRDALSL LDQAISHGAG
ETTVDQVRAM LGLADRGRVL DLFDMIMMGD AASALEELGG QYADGADPLA VLRDLAEITH
WVSVIKITPN AADDPTIGPD ERARGLAMAE KLPMRVLSRM WQMLLKAIEE VAAAPNAMMA
SEMAIIRLTH VADLPMPEDL VRKLNEQNPP PRPPSGPAGG GAPAGGGSVN AQGSTSAPRS
PVHGPTMSSG AATATAQAPD LALARYTSFQ SLVDLVGEHR DMKLKIDMET HMRIANYRPG
FIEFEPAGDA PSDLAQRLQS RLFAFTGQRW GVTIAKAPEG TETIREVADA ERLALEEEAK
QHPAIAKVFE LFPDAKITDI RTPEQIASEA AIEALQEVED EWDPFEE
//
