DNAA_GLUOX
ID DNAA_GLUOX Reviewed; 479 AA.
AC Q5FUU1;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377}; OrderedLocusNames=GOX0001;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
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:0000255|HAMAP-Rule:MF_00377}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00377}.
CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000255|HAMAP-
CC Rule:MF_00377}.
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DR EMBL; CP000009; AAW59800.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5FUU1; -.
DR SMR; Q5FUU1; -.
DR STRING; 290633.GOX0001; -.
DR EnsemblBacteria; AAW59800; AAW59800; GOX0001.
DR KEGG; gox:GOX0001; -.
DR eggNOG; COG0593; Bacteria.
DR HOGENOM; CLU_026910_3_0_5; -.
DR OMA; REFNPLF; -.
DR Proteomes; UP000006375; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 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; IPR024633; DnaA_N_dom.
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 Pfam; PF11638; DnaA_N; 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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA replication; DNA-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..479
FT /note="Chromosomal replication initiator protein DnaA"
FT /id="PRO_0000114184"
FT REGION 106..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 185..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
SQ SEQUENCE 479 AA; 53923 MW; A01C5267AA4F69B8 CRC64;
MKGGTMVENA QYLDASASAP GSTTPLETAW IRVREKLKSE VGEVEYRTWL RQIVLGPLEE
DELTLYLPTR FLRDWVRSQY EERLQTLWRT EREDIKGVEL QVKRGLPEVS MGDAEDGEDG
SGEGHELATQ AAAPESRSDL AVPLDPRFTF DTFIVGKPNE FAYACARRVA EKPSSPGFNP
LFLYGGVGLG KTHLMHAIGT ELTRTGKVSV AYMSAEKFMY RFIAAIRSQS TMEFKEQLRS
VDVLMIDDLQ FLIGKDNTQE EFFHTFNALV DAGRQIIVSA DKSPSDLSGL EDRLRTRLGC
GMVADIHATT FELRISILEA KAKASGTHVP SKVLEYLAHK ITTNVRELEG ALNRLIAHAD
LVGRPVTLDT TQDVLKDMLK AHDRRVTIEE IQRKVSEHWN IRLTDMSSAR RARAVARPRQ
VAMYLAKQLT SRSLPEIGRK FGNRDHTTVM HAVNRVTELM DQDTSFAEDV ELLRRMLEG