ID X7E7J7_9GAMM Unreviewed; 743 AA.
AC X7E7J7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=MUS1_08045 {ECO:0000313|EMBL:ETX11882.1};
OS Marinomonas ushuaiensis DSM 15871.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=1122207 {ECO:0000313|EMBL:ETX11882.1, ECO:0000313|Proteomes:UP000054058};
RN [1] {ECO:0000313|EMBL:ETX11882.1, ECO:0000313|Proteomes:UP000054058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15871 {ECO:0000313|EMBL:ETX11882.1,
RC ECO:0000313|Proteomes:UP000054058};
RA Lai Q., Shao Z.S.;
RT "Marinomonas ushuaiensis DSM 15871 Genome Sequencing.";
RL Submitted (JAN-2014) 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}.
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:ETX11882.1}.
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DR EMBL; JAMB01000002; ETX11882.1; -; Genomic_DNA.
DR RefSeq; WP_036159580.1; NZ_JAMB01000002.1.
DR AlphaFoldDB; X7E7J7; -.
DR STRING; 1122207.MUS1_08045; -.
DR PATRIC; fig|1122207.3.peg.924; -.
DR eggNOG; COG2812; Bacteria.
DR eggNOG; COG3115; Bacteria.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000054058; 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; 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 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:UP000054058};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..180
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 377..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 82007 MW; 312D88CD8EB137BB CRC64;
MSYQVLARKW RPQTFLEMAG QDHVLQALVN ALRQQRLHHA YLFTGTRGVG KTTIARIFAK
CLNCETNGIS PEPCGTCDSC REIVEGRFVD LIEVDAASRT KVEDTRELLE NVQYAPTRGR
FKVYLIDEVH MLSTHSFNAL LKTLEEPPAH VKFLLATTDP QKLPVTILSR CLQFNLKNMS
PQRVVDYLQT VLKSEQINFD QPALWQIGQA ANGSMRDALS LTDQAIAFGN GTISESGVTA
MLGLVNQAQV LDLLESVVSK NAADVLSRIS GLADYQPDFT AICGSLLECL HRVAIEQQVS
GALLDQLGDL ARIQGIAASV SSEEIQVMYQ NLLIGRRDLH LAHSARAGFE MLMLRLIAFR
PTPPMVVSHD VPPVVTAPQE VTEKKTPISD QVEEKKEANS EETPKKTPEK TPEKTQEAES
KYLSSQERPP WEDDPSINNA DPDVSIEPEI TANDSTDTDV ELSGEDDIPV DSIDPDITAL
DTVEIERKVE PETASSEFVE TPEITETEKV VETPEVVETS EALREHKPFV VAESEFSDDA
QEDEDEDEAE ERAIADVIDP FNPAADLVSA LSADAEALPV IEDEKEPDTR LSKIPDTIAQ
PALGMPMPEL NHYNELTMKH WWLVAPRLSL TGLVQNILMN SSLVDASDQG IRLEVPLEYG
HMLNQMRYEQ IQGALGGFFN MEVPLIIDTV EDTSGVTAEE FAASKRADAL QVAIEHLNSH
PVVQALSATM GAQLVYDTVK VKA
//
