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Database: UniProt
Entry: A0A2S9A9K3_9MICO
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ID   A0A2S9A9K3_9MICO        Unreviewed;       803 AA.
AC   A0A2S9A9K3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=CQ047_08250 {ECO:0000313|EMBL:PRB10176.1};
OS   Microbacterium sp. MYb72.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1848693 {ECO:0000313|EMBL:PRB10176.1, ECO:0000313|Proteomes:UP000238041};
RN   [1] {ECO:0000313|EMBL:PRB10176.1, ECO:0000313|Proteomes:UP000238041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MYb72 {ECO:0000313|EMBL:PRB10176.1,
RC   ECO:0000313|Proteomes:UP000238041};
RA   Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA   Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA   Kaleta C., Schulenburg H.;
RT   "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT   from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:PRB10176.1}.
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DR   EMBL; PCOT01000011; PRB10176.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S9A9K3; -.
DR   OrthoDB; 9810148at2; -.
DR   Proteomes; UP000238041; Unassembled WGS sequence.
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; 3.40.50.300; 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; 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   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022932};
KW   Transferase {ECO:0000256|ARBA:ARBA00022932}.
FT   DOMAIN          37..181
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          395..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          573..775
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..480
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..703
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        708..723
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   803 AA;  81560 MW;  1183EAAE84A3F4A2 CRC64;
     MVTTALYRRY RPESFGEMIG QSQVTDPLMT ALRGDRVGHA YLFSGPRGCG KTTSARILAR
     CLNCAEGPTD VPCGKCPSCI ELSRAGGGSL DVVEIDAASH NGVDDARDLR ERATFAPSRD
     RYKIFILDEA HMVTPQGFNA LLKLVEEPPE HVKFIFATTE PEKVLGTIRS RTHHYPFRLV
     PPAAMLEYVE KLCTEEGVVV EQGVLPLVVR AGGGSPRDTL SLLDQLIAGS DSPAGSETVT
     VAYERAVALL GYTHATVLDE IVDALAAGDA AAAFPAIDKV VQTGQDPRRF VDDLLERLRD
     LIVIAAVGAG ASAVLRGIAA DELDRMREQA ASFGSARLSR TADIVSAALD DMSGATSPRL
     HLELLVARVL AGGGADAAAP APVSAAARPA AAPAPASAAP APAASAPASA APAPATPASA
     PAAPAPAAPA AQTPAVQPSS APVVAPRGSG AGEAERGEIS VDSAAQPAPD SPSTSEAPAA
     ASAPAPSGPV TFERISGSWS AVLKRLEDIS RTSWLLATAV QPLAFDTASE VLTLGFTSQH
     DVQKFKGTVP GSGPSDHLRT AIEQELGVTV KYRPAPMPAG GAPRQPAAAS SPSSPSGDAP
     ASEPASAGSS RPQVRSDSAG PVTEWAVASI PSAGGQGAAS GGGAETPIPA ASTSAAPVPV
     TAASVHAAPT PATPSPSAPG STASAAPSAP ATSVSSSPTA ASPMSVDGPP LPDEPPYYDD
     EPPYDPAYEP AMSSAPPRRP EQSASAPTAA SAAPEPRRSA PAPVVTERTP AGGVQRYGEA
     VIRQVLGATF VREEPYEPPT RFS
//
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