ID Q63UU8_BURPS Unreviewed; 825 AA.
AC Q63UU8;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN Name=dnaX {ECO:0000313|EMBL:CAH35499.1};
GN OrderedLocusNames=BPSL1498 {ECO:0000313|EMBL:CAH35499.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH35499.1, ECO:0000313|Proteomes:UP000000605};
RN [1] {ECO:0000313|EMBL:CAH35499.1, ECO:0000313|Proteomes:UP000000605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243 {ECO:0000313|EMBL:CAH35499.1,
RC ECO:0000313|Proteomes:UP000000605};
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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 -!- SIMILARITY: Belongs to the DnaX/STICHEL family.
CC {ECO:0000256|ARBA:ARBA00006360}.
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DR EMBL; BX571965; CAH35499.1; -; Genomic_DNA.
DR RefSeq; WP_004555884.1; NZ_CP009538.1.
DR RefSeq; YP_108118.1; NC_006350.1.
DR AlphaFoldDB; Q63UU8; -.
DR SMR; Q63UU8; -.
DR STRING; 272560.BPSL1498; -.
DR KEGG; bps:BPSL1498; -.
DR PATRIC; fig|272560.51.peg.3534; -.
DR eggNOG; COG2812; Bacteria.
DR Proteomes; UP000000605; Chromosome 1.
DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:InterPro.
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 DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000313|EMBL:CAH35499.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000605};
KW Transferase {ECO:0000313|EMBL:CAH35499.1}.
FT DOMAIN 37..179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 420..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..679
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 825 AA; 84950 MW; 1255505C1171810D CRC64;
MTYQVLARKW RPKDFASLVG QEHVVRALTH ALDGGRLHHA YLFTGTRGVG KTTLSRIFAK
ALNCETGVTS QPCGVCRACR EIDEGRFVDY VEMDAASNRG VDEMAALLER AVYAPVDARF
KVYMIDEVHM LTNHAFNAML KTLEEPPPHV KFILATTDPQ KIPVTVLSRC LQFNLKQMPA
GHIVSHLERI LGEERIAFEP QALRLLARAA QGSMRDALSL TDQAIAYSAN EVTETAVSGM
LGTLDQTYMV RLLDALAAAD GPQILAVADE MALRSLSFSA ALQDLASLLH RIAWAQFAPA
SVLDEWPEAA DLRRFAELLS PEQVQLYYQI ATVGRGELGL APDEYAGFTM TLLRMLAFEP
ATTGGGAPAG GVPARVAGAA PKSGARAAAA VGASAVPAVT GATGATGAAL APKAAAARAA
TRAEAPPAAP ARPATAERGD DASDGDAPVP AKANARASAD SRCDERDAQP PADSGSASGA
SSSAPPDTAF ESAPRAAAPS AATPAAVPDA RAPAAASAED AVEAAAPAAP ESRPPTPAAG
APVSRATGAA AALDVLRNAG MRVSSGRGAG AARPAAGPAA SPTKPAPRVQ VSVPTPRARA
ATGDAPPNGA ARAEARAESR GAPPPWEDIP PDDYVPLSMD DGFIPPDDGF VPVFDGGPDD
VRVAPKPAPA PPVDTRPLPE PIPLDAIGYD GEWPTLAASL PLKGVAYQLA FNSELTAADG
GTLKLAVPVP QYADAAQVAK LKAALADALG KPVDVAVEVG PARRTAAALA AAERAKRQRE
AEQEMSADPF VQQLLREFGA SIVEGSIRPV GAEAGAADGA SPTLH
//
