ID A0A1F9X8K4_9BACT Unreviewed; 922 AA.
AC A0A1F9X8K4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 08-NOV-2023, entry version 26.
DE RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN ORFNames=A2314_01155 {ECO:0000313|EMBL:OGS23693.1};
OS Elusimicrobia bacterium RIFOXYB2_FULL_50_12.
OC Bacteria; Elusimicrobiota.
OX NCBI_TaxID=1797969 {ECO:0000313|EMBL:OGS23693.1, ECO:0000313|Proteomes:UP000176658};
RN [1] {ECO:0000313|EMBL:OGS23693.1, ECO:0000313|Proteomes:UP000176658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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.
CC {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377}.
CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC Rule:MF_00377, ECO:0000256|RuleBase:RU004227}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGS23693.1}.
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DR EMBL; MGVO01000086; OGS23693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F9X8K4; -.
DR STRING; 1797969.A2314_01155; -.
DR Proteomes; UP000176658; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR013317; DnaA.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00362; DnaA; 1.
DR PANTHER; PTHR30050; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 1.
DR PANTHER; PTHR30050:SF2; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 1.
DR Pfam; PF00308; Bac_DnaA; 1.
DR PRINTS; PR00051; DNAA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW ECO:0000256|RuleBase:RU000577};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377};
KW DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW ECO:0000256|RuleBase:RU000577};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW ECO:0000256|RuleBase:RU000577};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW ECO:0000256|RuleBase:RU000577}.
FT DOMAIN 506..634
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 217..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..451
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..773
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 514..521
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ SEQUENCE 922 AA; 102864 MW; 2256D8E26D3C682A CRC64;
MKKLRNWELS FYPSDTDSNR WRLKLKIDEK DLAVLLSSLP VKAGRPFIAE DDSFDFCLYL
YEVTINEFNQ VKGFLTEESP KGRVITSADK MKGGAVPFKT GSGAGQRPEK RIDSIWQLAF
SPNDKDKNRW CLKINIKEEE LNLLLGHMPG TKGRPFLLVN EPYTFGVYLY ELKDDSFKRV
KKLLEEEFLE GEILGPSKEE RLDALLEKVA KGLEQVHGDD KPVKEEVCEE QAPEDKVEKE
VTAEEPAVQN VVAEEKVSQD ATGEKNDEVV KPEDAPPPAP KGPGRPELII LHGKEVIPDP
AFGSPQPPEQ APQPPKSGFL SGWDILAAAR LRKLKKQEEK NETSSPAPEE KKVKPDVDVV
KEIEIVKVVE QPEPIATDEV KAAEEFTCIP PVVPEIPPIA EPEKNTEAAL EPDQPAEPQA
EQEPVIQVEP RQAPVPPVEP KQEPTPPPEK EIAPSQISFK NNEAPEATLQ DLELNPRYIF
EEFVIGPNNR FTAAAAQAVA DNPGKIYNPF FIYSGVGLGK THLMHAVGHY VHAKNPRMRI
LYVTTEKFMS EVIESIRHGT LQQMREHYRQ IDLLLIDDIQ FLVESESTQE EFFHTFNVLH
QSGKQIIITS DRTPKQLTTL EDRLRSRFEW GLIADIKSPN LETRVAILKK KGAVDNMELN
DNILLYIASK LKSNIRELEG FLKRINAYAS LTHQAVNMEL VRTLMSDLLP PGEMDDDLSQ
ETPAAPAPKA AASVDFSRPS PPPVTYAPPE HDARAPAPAP VPPPLPSPVP PSVKIPSTTS
SYSGTAADAS EANLKAVEVG FFFPEGKEGD LGNVKEHFRE VIKKHRLKFR LEGMFERSYP
VSAKVDYAAL VELCKASKVS IAIVIGPPPE SGIDPEEFAN LLATIMDDER ISLQLVPWAE
LNKDYRYLNL ALDITLLKHS SG
//
