DPO3A_TREPA
ID DPO3A_TREPA Reviewed; 1170 AA.
AC O83675;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=DNA polymerase III subunit alpha;
DE EC=2.7.7.7;
GN Name=dnaE; OrderedLocusNames=TP_0669;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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. The alpha chain
CC is the DNA polymerase (By similarity). {ECO:0000250}.
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 -!- 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 complex
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC subfamily. {ECO:0000305}.
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DR EMBL; AE000520; AAC26567.1; -; Genomic_DNA.
DR PIR; H71295; H71295.
DR RefSeq; WP_010882114.1; NC_021490.2.
DR AlphaFoldDB; O83675; -.
DR SMR; O83675; -.
DR IntAct; O83675; 2.
DR STRING; 243276.TPANIC_0669; -.
DR PRIDE; O83675; -.
DR EnsemblBacteria; AAC26567; AAC26567; TP_0669.
DR GeneID; 57879193; -.
DR KEGG; tpa:TP_0669; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_12; -.
DR OMA; NECRRMG; -.
DR OrthoDB; 561611at2; -.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008408; F:3'-5' exonuclease activity; 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 Gene3D; 1.10.10.1600; -; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR041931; DNA_pol3_alpha_thumb_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR InterPro; IPR004805; PolC_alpha.
DR PANTHER; PTHR32294; PTHR32294; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 1.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; SSF89550; 1.
DR TIGRFAMs; TIGR00594; polc; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA replication; DNA-directed DNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..1170
FT /note="DNA polymerase III subunit alpha"
FT /id="PRO_0000103356"
SQ SEQUENCE 1170 AA; 132313 MW; 431FC4629FDE09F1 CRC64;
MARMSFVHLH VHSNYSLLDG ASSLQRLVRT AKSLGQEALA LTDHGNMFGA LHFQKVCSAE
GIKAIIGCEL YVAPESRFDR SEHTIGRRYY HLIVLAKNET GYRNLMVLSS KAYIEGMYYK
PRVDDELLAQ HAEGLICLSS CLAGQLPYLL LQGRKREAEE HARKYRALFG VDNYFIEVQD
HGLDEEKKVA PLLIELACRL GIPLVVTNDV HYAEQEDSVA QDILLCIGTK KNRSDPNRLK
FKTDEFYLKS SEKMAQLFPH YPEMVLNTVR IAQRCNVRIP QPGPLLPLYQ IPHEFSSKEH
YIRHLVHRGL YDRYAVVSEE IKARADYELD VIVRMDFVGY FLIVWDFITW AKEHDIPVGP
GRGSGASSIV AYALKITDID PLRYKLLFER FMNPERISMP DFDIDFCFER RQEVIEYVRA
RYGNDNVGQI ITFGTLKPKA AIRDVGRVLD IPLSEVLMIT KLMPDDPKLT FKKAYESEQL
AQMKQEPRYA ELFQIAEKLE DTNRNTSLHA AGIVIGKTAL TDYVPLYKDS KTGKISTQFG
MDLIEDCGLV KMDFLGLKTL TLIQRTQNLV RRKGGKYTTF SISDISDQDP TTFSMLAEGK
SAAVFQFESR GMQGILKRAK PSKMEDLIAL NALYRPGPMA FIDQYIESKR DPGKIKYPDP
CLEDILSETY GVIVYQEQVM QVAQRIAGFS LGEADILRRA MGKKKLAVMQ EKKKEFAERA
EKQGFDKKHA ENIFEILIPF AGYGFNKSHA TAYSVVAYQT AFLKANFPAE FMAANLSNEI
NSAEKLPLYM AEAEKMGLSI QKPDVNASEP YFSVCEGCIV YGLLGIKGLG EQVAFDVFDE
RIRNGPYTSF VEVLDRVPAT SLNKKNAEIM IKAGCFDRFG VTRASLTAHL DDAMKYVARK
KAVTSSRQAS LFDETDLGEC SEYTFPVMEE WSQRERLRIE KELMGYYISG HPLDEYRSVI
GEKATLDLGH IENARSENKY LIVGVLNAIH PYTTKSGKNM AFGSFEDLHG SVDIVVFPVL
WEEHRAQFLP ETIMGLVGTV DFSKETPAFL VDSVIDLEQL RFAQVKTILA GSEHRRVSSG
EKTPLQKRGV SQEVHIEVSS HVRAHAQFKS LYEILSAHTG GSGEVFLHMH VDDRTYVVYV
PSCKVSATEV FAQQLKGNES FVQILKECVQ