ID Q7UWY5_RHOBA Unreviewed; 591 AA.
AC Q7UWY5;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|RuleBase:RU000577};
GN Name=dnaA {ECO:0000313|EMBL:CAD72227.1};
GN OrderedLocusNames=RB1706 {ECO:0000313|EMBL:CAD72227.1};
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD72227.1, ECO:0000313|Proteomes:UP000001025};
RN [1] {ECO:0000313|EMBL:CAD72227.1, ECO:0000313|Proteomes:UP000001025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1
RC {ECO:0000313|Proteomes:UP000001025};
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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|RuleBase:RU000577}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|ARBA:ARBA00006583,
CC ECO:0000256|RuleBase:RU004227}.
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DR EMBL; BX294135; CAD72227.1; -; Genomic_DNA.
DR RefSeq; NP_864546.1; NC_005027.1.
DR AlphaFoldDB; Q7UWY5; -.
DR STRING; 243090.RB1706; -.
DR EnsemblBacteria; CAD72227; CAD72227; RB1706.
DR KEGG; rba:RB1706; -.
DR PATRIC; fig|243090.15.peg.790; -.
DR eggNOG; COG0593; Bacteria.
DR HOGENOM; CLU_461434_0_0_0; -.
DR InParanoid; Q7UWY5; -.
DR OrthoDB; 9807019at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
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:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd06571; Bac_DnaA_C; 1.
DR Gene3D; 1.10.1750.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR020591; Chromosome_initiator_DnaA-like.
DR InterPro; IPR013317; DnaA.
DR InterPro; IPR013159; DnaA_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010921; Trp_repressor/repl_initiator.
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 Pfam; PF08299; Bac_DnaA_C; 1.
DR PRINTS; PR00051; DNAA.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00760; Bac_DnaA_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48295; TrpR-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000577};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU000577};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000577};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000577};
KW Reference proteome {ECO:0000313|Proteomes:UP000001025}.
FT DOMAIN 277..410
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 489..558
FT /note="Chromosomal replication initiator DnaA C-terminal"
FT /evidence="ECO:0000259|SMART:SM00760"
FT REGION 111..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 591 AA; 63529 MW; 1168B3F14E82343F CRC64;
MLTKSMREVC ATGMSSTQGS IETQEAIERF AEALHQRIGA DRYRLWFTHG VGFDLEVGES
PDDGKPTVVV VIRTSGPFAA QRMGNSFATE LRAAAMIACG ERARYRIDVE EAAQPEPKKR
TRAAKVAAEK KATTKSGARR SSTRQTSTRA TAGRQSGGRQ SSGRRGSANS LASLLAQSTA
TGSDQSGGSR GGKGRSRGRV EHDPIAASEL PTDERFDDEE IEDEEVAVST PRSSKSKLPP
LPESQPTGGR TLDSFITGPC NEFAFSAAMM AVATPSVATP LFLHGPTGTG KSHLLAALAN
EFRTRRRMRR VVLLTAEQFT NDFVVSVGST GLPAFRRRYR DVDALLIDDV HFLAAKTATL
REALYTVETL ASAGKPLVFS ANLPPSDIRG LTGEVAGRMA SGLVCPLAAL DQETRFKLLQ
RMVATRCVLG CDNTLLEEVS ELIGGDARAA GGIANLIGML QRMFRREPTI DEIRRYGGDL
LRSTQVAPTL RSIEKAVCET FGLEGDGLRG KAQTRRVSEP RTLAMYLARQ HTGSAFTEIA
KHFGRRSHSN AISAISKVET WLSSGKPIGA GDGAMSAQDA IARVESRLRV G
//
