ID B6IVU9_RHOCS Unreviewed; 507 AA.
AC B6IVU9;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|ARBA:ARBA00018893, ECO:0000256|HAMAP-Rule:MF_00377};
GN Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN ECO:0000313|EMBL:ACJ00423.1};
GN OrderedLocusNames=RC1_3057 {ECO:0000313|EMBL:ACJ00423.1};
OS Rhodospirillum centenum (strain ATCC 51521 / SW).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=414684 {ECO:0000313|EMBL:ACJ00423.1, ECO:0000313|Proteomes:UP000001591};
RN [1] {ECO:0000313|Proteomes:UP000001591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RA Touchman J.W., Bauer C., Blankenship R.E.;
RT "Genome sequence of Rhodospirillum centenum.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACJ00423.1, ECO:0000313|Proteomes:UP000001591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RX PubMed=20500872; DOI=10.1186/1471-2164-11-325;
RA Lu Y.K., Marden J., Han M., Swingley W.D., Mastrian S.D., Chowdhury S.R.,
RA Hao J., Helmy T., Kim S., Kurdoglu A.A., Matthies H.J., Rollo D.,
RA Stothard P., Blankenship R.E., Bauer C.E., Touchman J.W.;
RT "Metabolic flexibility revealed in the genome of the cyst-forming alpha-1
RT proteobacterium Rhodospirillum centenum.";
RL BMC Genomics 11:325-325(2010).
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|ARBA:ARBA00024640, ECO:0000256|HAMAP-Rule:MF_00377,
CC ECO:0000256|RuleBase:RU000577}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00377}.
CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|ARBA:ARBA00006583,
CC ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU004227}.
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DR EMBL; CP000613; ACJ00423.1; -; Genomic_DNA.
DR RefSeq; WP_012568203.1; NC_011420.2.
DR AlphaFoldDB; B6IVU9; -.
DR STRING; 414684.RC1_3057; -.
DR KEGG; rce:RC1_3057; -.
DR eggNOG; COG0593; Bacteria.
DR HOGENOM; CLU_026910_3_0_5; -.
DR OrthoDB; 9807019at2; -.
DR Proteomes; UP000001591; Chromosome.
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 CDD; cd06571; Bac_DnaA_C; 1.
DR Gene3D; 1.10.1750.10; -; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.300.180; -; 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; 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 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 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48295; TrpR-like; 1.
DR PROSITE; PS01008; DNAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00377};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00377};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00377};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00377};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00377}; Reference proteome {ECO:0000313|Proteomes:UP000001591}.
FT DOMAIN 204..332
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 415..484
FT /note="Chromosomal replication initiator DnaA C-terminal"
FT /evidence="ECO:0000259|SMART:SM00760"
FT REGION 87..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 212..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ SEQUENCE 507 AA; 56597 MW; CDF3F517BFF677A2 CRC64;
MSVQQGSLDQ QWAKVRGRLK DEVGETAYRS WLKPLTVGDF DGGQVRIMVP TRFMRDWIRT
HYADRIRALW SGENPGVQSV EIVVATSQKS ETRASEPPAS EIRASEIRAP ETRAPASGPA
PARSRARAVA EPALDGAAAA VAPSAPAYAE AEPAPVAAVG GAEEREDLSA PLDPRFTFEN
FVVGKPNELA FAAARRVADA SAVTFNPLFL YGGVGLGKTH LMHAIAWHIR RKDPSRRVIY
LSAEKFMYQF IRALRFKDTM AFKEQFRSVD VLMIDDVQFI SGKDSTQEEF FHTFNALVDQ
NRQVIISADK SPSDLEGMEE RLRSRLGWGL VADIHPTTYE LRLGILQQKA DQMGAKIPQK
VLEFLAHKIT SNVRELEGAL NRIVAHAELV GRAITLESTQ EVLHDLLRAS NRRVTIEEIQ
KKVAEHFNIR LSDMSSARRA RAVARPRQVA MYLAKQLTQR SLPEIGRKFG DRDHTTVMHA
VRKVEELCGT DPAFAEDVEL LRRMLEG
//
