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Database: UniProt
Entry: D5AUY7_RHOCB
LinkDB: D5AUY7_RHOCB
Original site: D5AUY7_RHOCB 
ID   D5AUY7_RHOCB            Unreviewed;       457 AA.
AC   D5AUY7;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   25-OCT-2017, entry version 56.
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:SAAS00911680}.
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   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   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; 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:SAAS00911664};
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:SAAS00911684};
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
//
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