ID Q6ABA1_CUTAK Unreviewed; 957 AA.
AC Q6ABA1;
DT 13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2004, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN OrderedLocusNames=PPA0204 {ECO:0000313|EMBL:AAT81965.1};
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Cutibacterium.
OX NCBI_TaxID=267747 {ECO:0000313|EMBL:AAT81965.1, ECO:0000313|Proteomes:UP000000603};
RN [1] {ECO:0000313|EMBL:AAT81965.1, ECO:0000313|Proteomes:UP000000603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202 {ECO:0000313|Proteomes:UP000000603};
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Bruggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Durre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
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}.
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DR EMBL; AE017283; AAT81965.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6ABA1; -.
DR EnsemblBacteria; AAT81965; AAT81965; PPA0204.
DR KEGG; pac:PPA0204; -.
DR eggNOG; COG2812; Bacteria.
DR HOGENOM; CLU_006229_10_1_11; -.
DR Proteomes; UP000000603; Chromosome.
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:0000313|EMBL:AAT81965.1};
KW Transferase {ECO:0000313|EMBL:AAT81965.1}.
FT DOMAIN 141..289
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..79
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 103019 MW; 0A95B660BCA1C806 CRC64;
MDERAPEPGM ENEAVEPEVF EQDGPDLFGD EESPRPVMPP DEATPDDDLP SDPCDPGLLD
GPETPEEPDG LETDEDEEDG ADVIERVQEL IGEAPDSNPD DDLPELPLAL YRRYRPETFD
EVIGEDHVIE PLKRAILNNR VNHAYLFSGP RGCGKTTTAR ILARALNCEQ GPTPTPCGTC
QSCRDLACGG PGSIDVIEID AASHGGVDDA RDLRERAFFA PVHSRYKIYI IDEAHMVTPQ
GFNALLKLVE EPPPHVKFIF ATTEPEKVIG TIRSRTHHYP FRLVPPKVLV EYLAELCGKE
GIDVDHAVLP LVVRAGGGSV RDSLSVLDQL LGGAADGHVS YEQAAALLGY TPEALLDEIV
DAFAAGDAHQ VFATIDKVIE VGQDPRRFAE DLLRRMRDLV IVSAVPDACR SGLIDVSPEQ
ATRLAHQVSG FGAGELTRAA EVLATGLTNM RGTTAPRLHL ELMCSRILLP GADTDGRGIH
ARLERLERRI GVSGPVEEVE RAERPVTAQP PTRYADTPQQ ASPPQHWPAE NLQNPERRSA
PEHHDAPSPG QRPSGRPRPS RKDYRPGNQL AEQPPSNQHG DDGQMSQGPR QQGGPSTSQR
QQPRPQDHQP SQRDRQDTPP AQPQQPSAEQ GGRADDAINI TTLRREWPQV LEAVKDGGRV
AWMVLNQYAQ VLEVHGNQAT LGFSNIGARE NFAAGNYPKV LHDAVVKVLG VDLAFTAVVG
EPPAAVRPES HPAEFQSGPA AQEPPDDDPW EQGPHHQDST RGGEPSDPTH PGRDPQGRPG
DRQAISDDAS KDAPPPPVTS SHPSEAGDDD PAPDATTEDQ SADVRDEVVE SGPVAGAPDP
DSGGAAEPKP DLVPGQDHVE AAGRAESARQ IDPGGASSQG RPSAAAVSTA HRWSERAKGS
VRPLEVTSRS AQVEEPPDDG GEWDDTVVEE SNESPIDLIM RELGGVVIDT DGDSTAR
//
