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Database: UniProt
Entry: A0A1Q9JHQ5_9FIRM
LinkDB: A0A1Q9JHQ5_9FIRM
Original site: A0A1Q9JHQ5_9FIRM 
ID   A0A1Q9JHQ5_9FIRM        Unreviewed;       619 AA.
AC   A0A1Q9JHQ5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=BHK98_06415 {ECO:0000313|EMBL:OLR55730.1};
OS   Hornefia porci.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XIII. Incertae Sedis; Hornefia.
OX   NCBI_TaxID=2652292 {ECO:0000313|EMBL:OLR55730.1, ECO:0000313|Proteomes:UP000187404};
RN   [1] {ECO:0000313|EMBL:OLR55730.1, ECO:0000313|Proteomes:UP000187404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=68-3-10 {ECO:0000313|EMBL:OLR55730.1,
RC   ECO:0000313|Proteomes:UP000187404};
RX   PubMed=27613689;
RA   Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT   "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT   Transferases and Their Diversity in the Proximal Colon of Swine.";
RL   Appl. Environ. Microbiol. 82:6788-6798(2016).
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:OLR55730.1}.
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DR   EMBL; MJIE01000001; OLR55730.1; -; Genomic_DNA.
DR   RefSeq; WP_075712721.1; NZ_MJIE01000001.1.
DR   AlphaFoldDB; A0A1Q9JHQ5; -.
DR   STRING; 1261640.BHK98_06415; -.
DR   OrthoDB; 9810148at2; -.
DR   Proteomes; UP000187404; 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; 3.40.50.300; 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; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR02397; dnaX_nterm; 1.
DR   PANTHER; PTHR11669:SF0; PROTEIN STICHEL-LIKE 2; 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   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:UP000187404};
KW   Transferase {ECO:0000256|RuleBase:RU364063}.
FT   DOMAIN          93..244
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   619 AA;  67753 MW;  F015FDFBB8848F35 CRC64;
     MRLCDSTPAR QGEPCCGHPR RAESRGGSAG ENAGAGGQRG ERAGLYFVQK KKEGVMKQYL
     ALYRENRPET FSQVLGQEHI VKILRHQIAT DTVAHAYLFC GTRGTGKTTM ARILAKAVNC
     TGESGEKPCG VCDTCRDIAA GRYVDVVEID AASNNGVENV RDLRESVNYP PVVGRKKVYI
     IDEVHMMSTN AFNAFLKTLE EPPADVIFIL ATTDPEKLPP TILSRCMRLD FKRVSGREIR
     ENMRRICAAH GVEITEDALA LLAMNADGSV RDSLSLLEQC MSSGEPLLDR DVVLEFLGAA
     SVEFYADLTE RALEHDVAGA LLLLEEALQE GKDIRQLMRG WMEHYRSLLI AKFVKEPQDM
     LNMSLENIDL LKQQAGRIRL EALNRNIVTL ARTISDARYS TQARILMEVA IVTIAEDMEY
     AGRAGTQTGG AAAQPRRAAE AGRTSGGAAA GHDMRSRGTK TGSPGRSASP RAPRQETPAA
     ENSRLPKSAA ETAVGAGQAA ESVNTPAPVD SSDGLDEIWR DVCEADGLDQ LSAGATMRGA
     RLAAMNDREF KLIVTGDMVR RMLERNSEQI CDLMEQRTGR RRKMVVREMN QTENRSKDER
     LQQAASEAAS ILGTKVDIR
//
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