ID A0A063XXP7_9GAMM Unreviewed; 597 AA.
AC A0A063XXP7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=ADINL_2057 {ECO:0000313|EMBL:KDE38928.1};
OS Nitrincola lacisaponensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Nitrincola.
OX NCBI_TaxID=267850 {ECO:0000313|EMBL:KDE38928.1, ECO:0000313|Proteomes:UP000027318};
RN [1] {ECO:0000313|EMBL:KDE38928.1, ECO:0000313|Proteomes:UP000027318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4CA {ECO:0000313|EMBL:KDE38928.1,
RC ECO:0000313|Proteomes:UP000027318};
RX PubMed=16280482; DOI=10.1099/ijs.0.63647-0;
RA Dimitriu P.A., Shukla S.K., Conradt J., Marquez M.C., Ventosa A.,
RA Maglia A., Peyton B.M., Pinkart H.C., Mormile M.R.;
RT "Nitrincola lacisaponensis gen. nov., sp. nov., a novel alkaliphilic
RT bacterium isolated from an alkaline, saline lake.";
RL Int. J. Syst. Evol. Microbiol. 55:2273-2278(2005).
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}.
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:KDE38928.1}.
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DR EMBL; JMSZ01000032; KDE38928.1; -; Genomic_DNA.
DR RefSeq; WP_036547418.1; NZ_JMSZ01000032.1.
DR AlphaFoldDB; A0A063XXP7; -.
DR STRING; 267850.ADINL_2057; -.
DR PATRIC; fig|267850.7.peg.2025; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000027318; 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; 3.30.300.150; DNA polymerase III, tau subunit, domain V; 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; IPR021029; DNA_pol_III_tau_dom-5.
DR InterPro; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038249; PolIII_tau_V_sf.
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; PF12170; DNA_pol3_tau_5; 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 ECO:0000313|EMBL:KDE38928.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027318};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:KDE38928.1}.
FT DOMAIN 37..178
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 421..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 65260 MW; BA4643F9C2725DE2 CRC64;
MSYQVLARKW RPRKFSEMAG QEHVLRALVN ALDNDRLHHA YLFTGTRGVG KTSIARLFAK
ALNCEVGVSS EPCGVCTACR EIAEGRFVDL IEVDAASRTK VEDTRELLEN VQYAPSHGRY
KVYLIDEVHM LSSSSFNALL KTLEEPPPHV KFLLATTDPQ KLPVTVLSRC LQFNLKNLSP
QRIVEHLNYV LTEEQISFDE PALWLLARSA DGSMRDALSL TDQAIAFGSG SVSESDVRSM
LGSIDQRLVY QLLVALAQQN AQGVMDAVQS LSEFSPDYAA VLADLVSLLH RVALAQVLPG
AIDNSLGDQQ QIMELAGLLR PEDVQLFYQI GLMGRKDLPY APDLREGLEM VLLRMLAFRP
ASVVPTASSG PDVVAAQPAV PAAVAVPVVE SVVESVPAAV SEAPRAAEPV VAAVPTKEPV
AVDDVPPWED APPYLEAEPP LETEHPAPEA DPQPKKHEAA EVRPAATLAK LALHDWVTVA
PELPLVGMTA SICRNLSLEL SDAEQLIFHF TSEQGALMNA TQQSRIQDAL QQHLGVELQI
SFVQAEQTRE TPAQYSNRKK AERQAEAVVA MQKDPLVQRI IEQFSAELDT ASVRPID
//
