ID O67056_AQUAE Unreviewed; 235 AA.
AC O67056;
DT 01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 144.
DE SubName: Full=DNA replication protein DnaC {ECO:0000313|EMBL:AAC07013.1};
GN Name=dnaC {ECO:0000313|EMBL:AAC07013.1};
GN OrderedLocusNames=aq_910 {ECO:0000313|EMBL:AAC07013.1};
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324 {ECO:0000313|EMBL:AAC07013.1, ECO:0000313|Proteomes:UP000000798};
RN [1] {ECO:0000313|EMBL:AAC07013.1, ECO:0000313|Proteomes:UP000000798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5 {ECO:0000313|EMBL:AAC07013.1,
RC ECO:0000313|Proteomes:UP000000798};
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olson G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2] {ECO:0007829|PDB:3EC2, ECO:0007829|PDB:3ECC}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 43-226 IN COMPLEX WITH ADP AND
RP MG(2+).
RX PubMed=19013274; DOI=10.1016/j.cell.2008.09.058;
RA Mott M.L., Erzberger J.P., Coons M.M., Berger J.M.;
RT "Structural synergy and molecular crosstalk between bacterial helicase
RT loaders and replication initiators.";
RL Cell 135:623-634(2008).
CC -!- INTERACTION:
CC O67056; O67056: dnaC; NbExp=2; IntAct=EBI-2120435, EBI-2120435;
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DR EMBL; AE000657; AAC07013.1; -; Genomic_DNA.
DR PIR; E70378; E70378.
DR RefSeq; NP_213618.1; NC_000918.1.
DR RefSeq; WP_010880556.1; NC_000918.1.
DR PDB; 3EC2; X-ray; 2.70 A; A=43-221.
DR PDB; 3ECC; X-ray; 2.70 A; A=43-226.
DR PDBsum; 3EC2; -.
DR PDBsum; 3ECC; -.
DR AlphaFoldDB; O67056; -.
DR SMR; O67056; -.
DR STRING; 224324.aq_910; -.
DR EnsemblBacteria; AAC07013; AAC07013; aq_910.
DR KEGG; aae:aq_910; -.
DR eggNOG; COG1484; Bacteria.
DR HOGENOM; CLU_062999_3_2_0; -.
DR InParanoid; O67056; -.
DR OrthoDB; 9776217at2; -.
DR EvolutionaryTrace; O67056; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006260; P:DNA replication; IBA:GO_Central.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR002611; IstB_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR30050:SF4; ATP-BINDING PROTEIN RV3427C IN INSERTION SEQUENCE-RELATED; 1.
DR PANTHER; PTHR30050; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 1.
DR Pfam; PF01695; IstB_IS21; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3EC2, ECO:0007829|PDB:3ECC};
KW Metal-binding {ECO:0007829|PDB:3EC2, ECO:0007829|PDB:3ECC};
KW Nucleotide-binding {ECO:0007829|PDB:3EC2, ECO:0007829|PDB:3ECC};
KW Reference proteome {ECO:0000313|Proteomes:UP000000798}.
FT DOMAIN 78..213
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 45
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:3EC2, ECO:0007829|PDB:3ECC"
FT BINDING 54
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:3EC2, ECO:0007829|PDB:3ECC"
FT BINDING 89
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:3EC2, ECO:0007829|PDB:3ECC"
FT BINDING 90
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:3EC2"
FT BINDING 91
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:3EC2, ECO:0007829|PDB:3ECC"
FT BINDING 92
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:3EC2, ECO:0007829|PDB:3ECC"
FT BINDING 93
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:3EC2, ECO:0007829|PDB:3ECC"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:3ECC"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:3EC2"
FT BINDING 94
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:3EC2, ECO:0007829|PDB:3ECC"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:3ECC"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:3EC2"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:3EC2"
FT BINDING 226
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:3ECC"
SQ SEQUENCE 235 AA; 26934 MW; 75E2C714237C23A1 CRC64;
MQDTATCSIC QGTGFVKTED NKVRLCECRF KKRDVNRELN IPKRYWNANL DTYHPKNVSQ
NRALLTIRVF VHNFNPEEGK GLTFVGSPGV GKTHLAVATL KAIYEKKGIR GYFFDTKDLI
FRLKHLMDEG KDTKFLKTVL NSPVLVLDDL GSERLSDWQR ELISYIITYR YNNLKSTIIT
TNYSLQREEE SSVRISADLA SRLGENVVSK IYEMNELLVI KGSDLRKSKK LSTPS
//
