DPO3X_HAEIN
ID DPO3X_HAEIN Reviewed; 688 AA.
AC P43746;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=DNA polymerase III subunit tau/gamma;
DE EC=2.7.7.7;
GN Name=dnaX; OrderedLocusNames=HI_1229;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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 -!- 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 -!- 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 complex
CC (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: As has been shown for E.coli (strain K12) and suggested
CC for Salmonella typhimurium, the gamma subunit (approximately resides 1-
CC 430) might be generated by ribosomal frameshifting, leading to 2
CC protein products from 1 gene.
CC -!- SIMILARITY: Belongs to the DnaX/STICHEL family. {ECO:0000305}.
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DR EMBL; L42023; AAC22882.1; -; Genomic_DNA.
DR PIR; F64111; F64111.
DR RefSeq; NP_439385.1; NC_000907.1.
DR RefSeq; WP_005694291.1; NC_000907.1.
DR AlphaFoldDB; P43746; -.
DR SMR; P43746; -.
DR STRING; 71421.HI_1229; -.
DR PRIDE; P43746; -.
DR EnsemblBacteria; AAC22882; AAC22882; HI_1229.
DR KEGG; hin:HI_1229; -.
DR PATRIC; fig|71421.8.peg.1281; -.
DR eggNOG; COG2812; Bacteria.
DR HOGENOM; CLU_006229_6_0_6; -.
DR OMA; YALHQGN; -.
DR PhylomeDB; P43746; -.
DR BioCyc; HINF71421:G1GJ1-1260-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR CDD; cd18137; HLD_clamp_pol_III_gamma_tau; 1.
DR Gene3D; 3.30.300.150; -; 1.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF12169; DNA_pol3_gamma3; 1.
DR Pfam; PF12170; DNA_pol3_tau_5; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02397; dnaX_nterm; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; DNA-directed DNA polymerase;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..688
FT /note="DNA polymerase III subunit tau/gamma"
FT /id="PRO_0000105493"
FT REGION 452..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 688 AA; 77042 MW; DD3401A54C6C9A6F CRC64;
MSYQVLARKW RPKTFADVVG QEHIITALAN GLKDNRLHHA YLFSGTRGVG KTSIARLFAK
GLNCVHGVTA TPCGECENCK AIEQGNFIDL IEIDAASRTK VEDTRELLDN VQYKPVVGRF
KVYLIDEVHM LSRHSFNALL KTLEEPPEYV KFLLATTDPQ KLPVTILSRC LQFHLKALDE
TQISQHLAHI LTQENIPFED PALVKLAKAA QGSIRDSLSL TDQAIAMGDR QVTNNVVSNM
LGLLDDNYSV DILYALHQGN GELLMRTLQR VADAAGDWDK LLGECAEKLH QIALMQLLPQ
KSSDNNEHFS FLAKHISPEN VQFFYQVIVS GRKDLSNAPN RRIGAEMTLL RALAFHPKFL
TAVPKANTTI TPPPSTPSAV ENTGNYVDVP VLSQSIKSAY SQAKPNKTSI PNLASLSALD
ALEHLTQLEN QERQEHKAES LAVVSETLHH IQELDEEKSH KKMTALPVRE MTEPKPKHIE
KPTLPSNAAQ APQKNSTEEN SSDDNVEIAQ DEQEILSADT YRWEWSNPEL AKADTGVCPS
DIKQAILKDI TPELRLKIIT QTQQQDQWAD IVERSGLTGF SKELALNCFL QSKTDDEINL
GLHSEKSHLR QDRSIKNLAE ALSKLQGKDI RLTINLDDSN VTTPIEYRRN IYQALREKAQ
NELQKDSKLQ ILLNEFDAKL DVESIRPV
