ID Q87YZ3_PSESM Unreviewed; 743 AA.
AC Q87YZ3;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 136.
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=dnaZX {ECO:0000313|EMBL:AAO57116.1};
GN Synonyms=dnaX {ECO:0000256|RuleBase:RU364063};
GN OrderedLocusNames=PSPTO_3646 {ECO:0000313|EMBL:AAO57116.1};
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283 {ECO:0000313|EMBL:AAO57116.1, ECO:0000313|Proteomes:UP000002515};
RN [1] {ECO:0000313|EMBL:AAO57116.1, ECO:0000313|Proteomes:UP000002515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000 {ECO:0000313|Proteomes:UP000002515};
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., Deboy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S., Brinkac L., Beanan M.J., Haft D.H., Nelson W.C., Davidsen T.,
RA Zafar N., Zhou L., Liu J., Yuan Q., Khouri H., Fedorova N., Tran B.,
RA Russell D., Berry K., Utterback T., Van Aken S.E., Feldblyum T.V.,
RA D'Ascenzo M., Deng W.L., Ramos A.R., Alfano J.R., Cartinhour S.,
RA Chatterjee A.K., Delaney T.P., Lazarowitz S.G., Martin G.B.,
RA Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M., Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO57116.1; -; Genomic_DNA.
DR RefSeq; NP_793421.1; NC_004578.1.
DR RefSeq; WP_011104647.1; NC_004578.1.
DR AlphaFoldDB; Q87YZ3; -.
DR STRING; 223283.PSPTO_3646; -.
DR GeneID; 1185311; -.
DR KEGG; pst:PSPTO_3646; -.
DR PATRIC; fig|223283.9.peg.3735; -.
DR eggNOG; COG2812; Bacteria.
DR HOGENOM; CLU_006229_6_0_6; -.
DR OrthoDB; 9810148at2; -.
DR PhylomeDB; Q87YZ3; -.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0009360; C:DNA polymerase III complex; ISS:JCVI.
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; ISS:JCVI.
DR GO; GO:0006260; P:DNA replication; ISS:JCVI.
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 Reference proteome {ECO:0000313|Proteomes:UP000002515};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 362..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..451
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..529
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 80783 MW; ACCB626A1B18885A CRC64;
MSYQVLARKW RPRSFREMVG QAHVLKALIN ALDSQRLHHA YLFTGTRGVG KTTIARIIAK
CLNCETGITS TPCGTCSVCK EIDEGRFVDL IEIDAASRTK VEDTRELLDN VQYAPSRGRF
KVYLIDEVHM LSSHSFNALL KTLEEPPPYV KFILATTDPQ KLPATILSRC LQFSLKNMTP
ERVVEHLTHV LGVENVPFED DALWLLGRAA DGSMRDAMSL TDQAIAFGEG KVMAADVRAM
LGTLDHGQVF DVLTALLEGD ARGVLEAVRH LAEQGPDWNG VLSEILNVLH RVAIAQALPE
GVDNGHGDRD RVLALAQALP AEDVQFYYQM GLIGRRDLPL APDPRGGFEM VLLRMLAFRP
ADSEDAPRQP LKPVGISQAT ADSRKTVADA TPVASPASTP PVVAAPDPAF EAQPPAYAPA
PAAVQPEAKA EPAPQIKPEP EPQPEPKPAP VEEIDLPWNE SKAPVAEKPA EPEPEPEPEP
DPVAEVEAEP QPEPVAEPVL ETVSEQPDLT PMPAPAPASP VPDAPQAQPS PPVEEQQVTP
AMLEAIPDSA YLSAPMDRDD EPPADDDYVE PDIDIDPASY SYLDELAHES VVELEAVEPE
PAPAAMPATG LAADWLEVFP KLPISGMTGS IAANCTLMAV DGDNWLLHLD PAHSALFNST
QQRRLNDALN QYHGRTINLS IELIKPEQET PAQAASRLRT ERQRQAEASI QADPYIQQML
QQFGAVIRED TIKPVDAPVV QTQ
//
