DNAA_MYCTU
ID DNAA_MYCTU Reviewed; 507 AA.
AC P9WNW3; L0T412; P49993; P95309; Q59585;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Chromosomal replication initiator protein DnaA;
GN Name=dnaA; OrderedLocusNames=Rv0001; ORFNames=MTV029.01;
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 [GENOMIC DNA].
RA Qin M.H., Madiraju M.V., Rajagopalan M.;
RT "The dnaA gene region of M. tuberculosis.";
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=8733228; DOI=10.1111/j.1365-2958.1996.tb02617.x;
RA Salazar L., Fsihi H., De Rossi E., Riccardi G., Rios C., Cole S.T.,
RA Takiff H.E.;
RT "Organization of the origins of replication of the chromosomes of
RT Mycobacterium smegmatis, Mycobacterium leprae and Mycobacterium
RT tuberculosis and isolation of a functional origin from M. smegmatis.";
RL Mol. Microbiol. 20:283-293(1996).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 213-472.
RX PubMed=7557482; DOI=10.1016/0378-1119(95)00403-s;
RA Rajagopalan M., Qin M.H., Steingrube V.A., Nash D.R., Wallace R.J. Jr.,
RA Madiraju M.V.V.S.;
RT "Amplification and cloning of the Mycobacterium tuberculosis dnaA gene.";
RL Gene 163:75-79(1995).
RN [5]
RP INDUCTION, AND DNA-BINDING.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16629667; DOI=10.1111/j.1365-2958.2006.05137.x;
RA Fol M., Chauhan A., Nair N.K., Maloney E., Moomey M., Jagannath C.,
RA Madiraju M.V., Rajagopalan M.;
RT "Modulation of Mycobacterium tuberculosis proliferation by MtrA, an
RT essential two-component response regulator.";
RL Mol. Microbiol. 60:643-657(2006).
RN [6]
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).
CC -!- FUNCTION: Plays an important role in the initiation and regulation of
CC chromosomal replication. Binds to the origin of replication; it binds
CC specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-
CC TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids (By
CC similarity). Binds its own promoter. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Expression depends on the two-component regulatory system
CC MtrA/MtrB. {ECO:0000269|PubMed:16629667}.
CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000305}.
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DR EMBL; U38891; AAB38528.2; -; Genomic_DNA.
DR EMBL; X92504; CAA63257.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP42723.1; -; Genomic_DNA.
DR EMBL; U19184; AAA85543.1; -; Genomic_DNA.
DR PIR; S70982; S70982.
DR RefSeq; NP_214515.1; NC_000962.3.
DR RefSeq; WP_003400253.1; NZ_NVQJ01000005.1.
DR AlphaFoldDB; P9WNW3; -.
DR SMR; P9WNW3; -.
DR STRING; 83332.Rv0001; -.
DR PaxDb; P9WNW3; -.
DR DNASU; 885041; -.
DR GeneID; 45423958; -.
DR GeneID; 885041; -.
DR KEGG; mtu:Rv0001; -.
DR TubercuList; Rv0001; -.
DR eggNOG; COG0593; Bacteria.
DR OMA; REFNPLF; -.
DR PhylomeDB; P9WNW3; -.
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:0005524; F:ATP binding; IDA:MTBBASE.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:MTBBASE.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:MTBBASE.
DR GO; GO:0006172; P:ADP biosynthetic process; IDA:MTBBASE.
DR GO; GO:0016311; P:dephosphorylation; IDA:MTBBASE.
DR GO; GO:0006260; P:DNA replication; IBA:GO_Central.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd06571; Bac_DnaA_C; 1.
DR Gene3D; 1.10.1750.10; -; 1.
DR Gene3D; 3.30.300.180; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00377; DnaA_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR001957; Chromosome_initiator_DnaA.
DR InterPro; IPR020591; Chromosome_initiator_DnaA-like.
DR InterPro; IPR018312; Chromosome_initiator_DnaA_CS.
DR InterPro; IPR013317; DnaA.
DR InterPro; IPR013159; DnaA_C.
DR InterPro; IPR038454; DnaA_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010921; Trp_repressor/repl_initiator.
DR PANTHER; PTHR30050:SF2; PTHR30050:SF2; 1.
DR Pfam; PF00308; Bac_DnaA; 1.
DR Pfam; PF08299; Bac_DnaA_C; 1.
DR PRINTS; PR00051; DNAA.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00760; Bac_DnaA_C; 1.
DR SUPFAM; SSF48295; SSF48295; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00362; DnaA; 1.
DR PROSITE; PS01008; DNAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; DNA replication; DNA-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..507
FT /note="Chromosomal replication initiator protein DnaA"
FT /id="PRO_0000114218"
FT REGION 99..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 208..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 363
FT /note="S -> R (in Ref. 4; AAA85543)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="E -> V (in Ref. 4; AAA85543)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="A -> P (in Ref. 4; AAA85543)"
FT /evidence="ECO:0000305"
FT CONFLICT 429..430
FT /note="EE -> GR (in Ref. 4; AAA85543)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="M -> V (in Ref. 1; AAB38528)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="S -> P (in Ref. 4; AAA85543)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 56567 MW; C4F252150D453A00 CRC64;
MTDDPGSGFT TVWNAVVSEL NGDPKVDDGP SSDANLSAPL TPQQRAWLNL VQPLTIVEGF
ALLSVPSSFV QNEIERHLRA PITDALSRRL GHQIQLGVRI APPATDEADD TTVPPSENPA
TTSPDTTTDN DEIDDSAAAR GDNQHSWPSY FTERPHNTDS ATAGVTSLNR RYTFDTFVIG
ASNRFAHAAA LAIAEAPARA YNPLFIWGES GLGKTHLLHA AGNYAQRLFP GMRVKYVSTE
EFTNDFINSL RDDRKVAFKR SYRDVDVLLV DDIQFIEGKE GIQEEFFHTF NTLHNANKQI
VISSDRPPKQ LATLEDRLRT RFEWGLITDV QPPELETRIA ILRKKAQMER LAVPDDVLEL
IASSIERNIR ELEGALIRVT AFASLNKTPI DKALAEIVLR DLIADANTMQ ISAATIMAAT
AEYFDTTVEE LRGPGKTRAL AQSRQIAMYL CRELTDLSLP KIGQAFGRDH TTVMYAQRKI
LSEMAERREV FDHVKELTTR IRQRSKR
