ID D7H7Q4_VIBCL Unreviewed; 692 AA.
AC D7H7Q4;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=VCRC385_00717 {ECO:0000313|EMBL:EFH75085.1};
OS Vibrio cholerae RC385.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345074 {ECO:0000313|EMBL:EFH75085.1, ECO:0000313|Proteomes:UP000004696};
RN [1] {ECO:0000313|Proteomes:UP000004696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RC385 {ECO:0000313|Proteomes:UP000004696};
RA Heidelberg J.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EFH75085.1, ECO:0000313|Proteomes:UP000004696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RC385 {ECO:0000313|EMBL:EFH75085.1,
RC ECO:0000313|Proteomes:UP000004696};
RG The Broad Institute Genome Sequencing Platform;
RA Colwell R., Grim C.J., Young S., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.,
RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Walk T., White J., Yandava C., Borodovsky M.,
RA Heidelberg J., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Vibrio cholerae RC385.";
RL Submitted (OCT-2009) 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}.
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DR EMBL; GG774555; EFH75085.1; -; Genomic_DNA.
DR RefSeq; WP_000120794.1; NZ_GG774555.1.
DR AlphaFoldDB; D7H7Q4; -.
DR PATRIC; fig|345074.23.peg.3011; -.
DR HOGENOM; CLU_006229_6_0_6; -.
DR Proteomes; UP000004696; 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; IPR022001; DNA_pol3_tau_IV.
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; PF12168; DNA_pol3_tau_4; 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 Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 385..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 692 AA; 76133 MW; 81442B5F3E48411A CRC64;
MSYLALARKW RPTRFSEVVG QSHVLTALEN ALAQNRLHHA YLFSGTRGVG KTTIGRLFAK
GLNCETGITA TPCGQCATCQ EIDQGRFVDL LEIDAASRTK VEDTRELLDN VQYKPARGRF
KVYLIDEVHM LSRHSFNALL KTLEEPPEYV KFLLATTDPQ KLPVTILSRC LQFHLKPISV
ENIQQQLDKV LHAEQISSDS KALNLLAHAA DGSMRDALSL TDQAIALGNG VVKSDIVAHM
LGTLDTDHAL HLLQAISLQT PQAVMDCIET LAQNGVEWDG LLQQLSTQLH RIAMYQALPA
TLDKSLPEAS RIESLAKTLA PQDVQLYYQI ALKGRQDLPL SPTARIGIEM LMLRMMAFRP
SHVSLASVIV PPNTAVTAPT ITAPTSQTAT SAPQPQPVAQ SNVSQPASQA MPHPVAPPMM
AAQPVVESAV PVTQREASHS INAPEVSVVT NTDTQSQASM PALAGLRHQL RSKRQEVQNK
GADGKKSDAT SATPASALER IAQRAQQVQV SPERNDEDEL EPEEEIYQWR PMQPIEVAVK
SEVTPTQLKK ALEHEKTPEM VAKLIEEAVA QDAWSALVQR LETAKMVEQL ALNSAFVRQG
DQISLTLRPS HAHLHNEKAQ QELEQALNHV LGEACSLNIT VGQEGEPPLE LRERLYQQKL
TSALHSLQTD PNVQFIERRF NAQLDSDSVR PI
//
