DPO3A_MYCTU
ID DPO3A_MYCTU Reviewed; 1184 AA.
AC P9WNT7; L0T6Z6; P63977; Q10779;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=DNA polymerase III subunit alpha;
DE EC=2.7.7.7;
GN Name=dnaE1; Synonyms=dnaE; OrderedLocusNames=Rv1547; ORFNames=MTCY48.18c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP SUBUNIT.
RC STRAIN=H37Rv;
RX PubMed=32634279; DOI=10.1111/mmi.14571;
RA Zaveri A., Wang R., Botella L., Sharma R., Zhu L., Wallach J.B., Song N.,
RA Jansen R.S., Rhee K.Y., Ehrt S., Schnappinger D.;
RT "Depletion of the DarG antitoxin in Mycobacterium tuberculosis triggers the
RT DNA-damage response and leads to cell death.";
RL Mol. Microbiol. 114:641-652(2020).
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|UniProtKB:P10443}.
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). Co-immunoprecipitates with DarG in the presence and
CC absence of darT (PubMed:32634279). {ECO:0000250|UniProtKB:P10443,
CC ECO:0000269|PubMed:32634279}.
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; AL123456; CCP44311.1; -; Genomic_DNA.
DR PIR; H70761; H70761.
DR RefSeq; NP_216063.1; NC_000962.3.
DR RefSeq; WP_003407751.1; NZ_NVQJ01000004.1.
DR PDB; 5LEW; X-ray; 2.80 A; A=7-933.
DR PDBsum; 5LEW; -.
DR AlphaFoldDB; P9WNT7; -.
DR SMR; P9WNT7; -.
DR IntAct; P9WNT7; 1.
DR STRING; 83332.Rv1547; -.
DR PaxDb; P9WNT7; -.
DR GeneID; 886392; -.
DR KEGG; mtu:Rv1547; -.
DR TubercuList; Rv1547; -.
DR eggNOG; COG0587; Bacteria.
DR OMA; NECRRMG; -.
DR PhylomeDB; P9WNT7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA replication; DNA-directed DNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..1184
FT /note="DNA polymerase III subunit alpha"
FT /id="PRO_0000103329"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:5LEW"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:5LEW"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:5LEW"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 115..131
FT /evidence="ECO:0007829|PDB:5LEW"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:5LEW"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 172..186
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:5LEW"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 201..217
FT /evidence="ECO:0007829|PDB:5LEW"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:5LEW"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 268..275
FT /evidence="ECO:0007829|PDB:5LEW"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 282..292
FT /evidence="ECO:0007829|PDB:5LEW"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 317..332
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 341..355
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 358..373
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 383..387
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 389..393
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 401..404
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 408..411
FT /evidence="ECO:0007829|PDB:5LEW"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 431..442
FT /evidence="ECO:0007829|PDB:5LEW"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:5LEW"
FT STRAND 447..455
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 458..470
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 475..483
FT /evidence="ECO:0007829|PDB:5LEW"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 496..499
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 513..519
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 521..531
FT /evidence="ECO:0007829|PDB:5LEW"
FT TURN 532..535
FT /evidence="ECO:0007829|PDB:5LEW"
FT STRAND 537..549
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 554..556
FT /evidence="ECO:0007829|PDB:5LEW"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:5LEW"
FT TURN 564..566
FT /evidence="ECO:0007829|PDB:5LEW"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 575..579
FT /evidence="ECO:0007829|PDB:5LEW"
FT TURN 580..582
FT /evidence="ECO:0007829|PDB:5LEW"
FT STRAND 584..591
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 592..608
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 622..630
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 642..651
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 656..665
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 668..672
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 675..683
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 694..700
FT /evidence="ECO:0007829|PDB:5LEW"
FT TURN 701..709
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 714..725
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 729..741
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 744..760
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 765..781
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 785..804
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 806..816
FT /evidence="ECO:0007829|PDB:5LEW"
FT TURN 817..819
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 821..833
FT /evidence="ECO:0007829|PDB:5LEW"
FT STRAND 837..839
FT /evidence="ECO:0007829|PDB:5LEW"
FT TURN 843..845
FT /evidence="ECO:0007829|PDB:5LEW"
FT STRAND 851..853
FT /evidence="ECO:0007829|PDB:5LEW"
FT STRAND 856..858
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 869..881
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 888..894
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 899..910
FT /evidence="ECO:0007829|PDB:5LEW"
FT TURN 911..914
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 915..917
FT /evidence="ECO:0007829|PDB:5LEW"
FT HELIX 921..932
FT /evidence="ECO:0007829|PDB:5LEW"
SQ SEQUENCE 1184 AA; 129323 MW; A87AB7F0F2E08909 CRC64;
MSGSSAGSSF VHLHNHTEYS MLDGAAKITP MLAEVERLGM PAVGMTDHGN MFGASEFYNS
ATKAGIKPII GVEAYIAPGS RFDTRRILWG DPSQKADDVS GSGSYTHLTM MAENATGLRN
LFKLSSHASF EGQLSKWSRM DAELIAEHAE GIIITTGCPS GEVQTRLRLG QDREALEAAA
KWREIVGPDN YFLELMDHGL TIERRVRDGL LEIGRALNIP PLATNDCHYV TRDAAHNHEA
LLCVQTGKTL SDPNRFKFDG DGYYLKSAAE MRQIWDDEVP GACDSTLLIA ERVQSYADVW
TPRDRMPVFP VPDGHDQASW LRHEVDAGLR RRFPAGPPDG YRERAAYEID VICSKGFPSY
FLIVADLISY ARSAGIRVGP GRGSAAGSLV AYALGITDID PIPHGLLFER FLNPERTSMP
DIDIDFDDRR RGEMVRYAAD KWGHDRVAQV ITFGTIKTKA ALKDSARIHY GQPGFAIADR
ITKALPPAIM AKDIPLSGIT DPSHERYKEA AEVRGLIETD PDVRTIYQTA RGLEGLIRNA
GVHACAVIMS SEPLTEAIPL WKRPQDGAII TGWDYPACEA IGLLKMDFLG LRNLTIIGDA
IDNVRANRGI DLDLESVPLD DKATYELLGR GDTLGVFQLD GGPMRDLLRR MQPTGFEDVV
AVIALYRPGP MGMNAHNDYA DRKNNRQAIK PIHPELEEPL REILAETYGL IVYQEQIMRI
AQKVASYSLA RADILRKAMG KKKREVLEKE FEGFSDGMQA NGFSPAAIKA LWDTILPFAD
YAFNKSHAAG YGMVSYWTAY LKANYPAEYM AGLLTSVGDD KDKAAVYLAD CRKLGITVLP
PDVNESGLNF ASVGQDIRYG LGAVRNVGAN VVGSLLQTRN DKGKFTDFSD YLNKIDISAC
NKKVTESLIK AGAFDSLGHA RKGLFLVHSD AVDSVLGTKK AEALGQFDLF GSNDDGTGTA
DPVFTIKVPD DEWEDKHKLA LEREMLGLYV SGHPLNGVAH LLAAQVDTAI PAILDGDVPN
DAQVRVGGIL ASVNRRVNKN GMPWASAQLE DLTGGIEVMF FPHTYSSYGA DIVDDAVVLV
NAKVAVRDDR IALIANDLTV PDFSNAEVER PLAVSLPTRQ CTFDKVSALK QVLARHPGTS
QVHLRLISGD RITTLALDQS LRVTPSPALM GDLKELLGPG CLGS
