ID D5AUY7_RHOCB Unreviewed; 457 AA.
AC D5AUY7;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 28-MAR-2018, entry version 58.
DE RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724181};
GN Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN ECO:0000313|EMBL:ADE83766.1};
GN OrderedLocusNames=RCAP_rcc00001 {ECO:0000313|EMBL:ADE83766.1};
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942 {ECO:0000313|EMBL:ADE83766.1, ECO:0000313|Proteomes:UP000002361};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SB1003;
RA Strnad H., Lapidus A., Vlcek C., Ulbrich P., Paces J., Maltsev N.,
RA Kumar V., Kogan Y., Milgram A., Rebrekov D., Mazur M., Cox R.,
RA Kyrpides N., Kolar M., Sachova J., Ridl J., Ivanova N., Kapatral V.,
RA Los T., Lykidis A., Mikhailova N., Reznik G., Vasieva O., Fonstein M.,
RA Paces V., Haselkorn R.;
RT "Complete genome sequence of Rhodobacter capsulatus SB1003.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADE83766.1, ECO:0000313|Proteomes:UP000002361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003
RC {ECO:0000313|Proteomes:UP000002361};
RX PubMed=20418398; DOI=10.1128/JB.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur
RT bacterium Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
CC -!- FUNCTION: Plays an important role in the initiation and regulation
CC of chromosomal replication. Binds to the origin of replication; it
CC binds specifically double-stranded DNA at a 9 bp consensus (dnaA
CC box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic
CC phospholipids. {ECO:0000256|HAMAP-Rule:MF_00377,
CC ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724167}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC ECO:0000256|SAAS:SAAS00747961}.
CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC ECO:0000256|SAAS:SAAS00555179}.
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DR EMBL; CP001312; ADE83766.1; -; Genomic_DNA.
DR RefSeq; WP_013065748.1; NC_014034.1.
DR STRING; 272942.RCAP_rcc00001; -.
DR EnsemblBacteria; ADE83766; ADE83766; RCAP_rcc00001.
DR GeneID; 31488958; -.
DR KEGG; rcp:RCAP_rcc00001; -.
DR eggNOG; ENOG4105CI4; Bacteria.
DR eggNOG; COG0593; LUCA.
DR HOGENOM; HOG000235660; -.
DR KO; K02313; -.
DR OMA; REFNPLF; -.
DR OrthoDB; POG091H02FF; -.
DR BioCyc; RCAP272942:G1GUE-1-MONOMER; -.
DR Proteomes; UP000002361; 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 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 {ECO:0000256|HAMAP-Rule:MF_00377,
KW ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747950};
KW Complete proteome {ECO:0000313|Proteomes:UP000002361};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW ECO:0000256|SAAS:SAAS00747973};
KW DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00748008};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW Reference proteome {ECO:0000313|Proteomes:UP000002361}.
FT DOMAIN 149 279 AAA. {ECO:0000259|SMART:SM00382}.
FT DOMAIN 365 434 Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT NP_BIND 157 164 ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ SEQUENCE 457 AA; 51562 MW; 45AE7D4EF513A1E2 CRC64;
MTNELWGQVC NELQRTVGRT NFNTWIAPLQ LIELSDGIVS FEAPTKFMCD WVSRNYGEPI
LRELRNSGMA VERVAIRVPE GRPMPAPEAR PMPEKAPAPA RKAARVSEDQ DLPGAPLDAR
FTFDSFVVGK PNELAHAAAR RVAEGGPVTF NPLFLYGGVG LGKTHLMHAI AHELQTQHGE
LRVLYLSAEQ FMYRFVQALR DRQIMDFKEL FRSVDVLMVD DVQFIAGKDS TQEEFFHTFN
ALVDQGKQIV ISADRAPGEI KDLEDRIKSR LQCGLVVDLH PTDYELRLGI LQTKTEIHAA
RNPGLVVASG VLEFLAHRIT TNVRVLEGAL TRLFAFASLV GREITLDLAQ ECLADILRAS
DRRVTIEEIQ RKVAEHYNVR LSDMIGPKRL RTIARPRQVA MYLSKHLTTR SLPEIGRRFG
GRDHTTIMHG IRKIDELMTT DRQLAEDIGL LKRLMES
//
