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Database: UniProt
Entry: A3K331_9RHOB
LinkDB: A3K331_9RHOB
Original site: A3K331_9RHOB 
ID   A3K331_9RHOB            Unreviewed;       459 AA.
AC   A3K331;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   25-OCT-2017, entry version 65.
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   ORFNames=SSE37_17298 {ECO:0000313|EMBL:EBA08590.1};
OS   Sagittula stellata E-37.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Sagittula.
OX   NCBI_TaxID=388399 {ECO:0000313|EMBL:EBA08590.1, ECO:0000313|Proteomes:UP000005713};
RN   [1] {ECO:0000313|EMBL:EBA08590.1, ECO:0000313|Proteomes:UP000005713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E-37 {ECO:0000313|EMBL:EBA08590.1,
RC   ECO:0000313|Proteomes:UP000005713};
RA   Moran M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EBA08590.1}.
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DR   EMBL; AAYA01000005; EBA08590.1; -; Genomic_DNA.
DR   RefSeq; WP_005858584.1; NZ_AAYA01000005.1.
DR   ProteinModelPortal; A3K331; -.
DR   STRING; 388399.SSE37_17298; -.
DR   EnsemblBacteria; EBA08590; EBA08590; SSE37_17298.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000005713; Unassembled WGS sequence.
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:UP000005713};
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:UP000005713}.
FT   DOMAIN      151    281       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      367    436       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     159    166       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   459 AA;  52060 MW;  16B6875B44CA6129 CRC64;
     MKKEQWGALQ EQICKTIGQN NYKTWIQPLR FRGITADGIV TLQAPTNFFG TYVSQNFGDM
     LLAQISTVEP SARRLAFQAG ILDDSSEDAE EKAKPLNIPE AEQAPVTSSR DQQLPGAPLD
     MRFTFDTFVV GKPNELAHAA ARRVAEGGPV TFNPLFLYGG VGLGKTHLMH AIAWELSQRN
     PGLTVLYLSA EQFMYRFVQA LRERKMMDFK EMFRSVDVLM VDDVQFIAGK DSTQEEFFHT
     FNALVDQNKQ IIISADRAPD EIKDLENRIR SRLQSGLVVD LHPTDYELRL GILQSKVEVY
     RGMHPGLQID DGVLEFLAHR ISTNVRVLEG ALTRLFAFAS LVGKPINMDL VQDSLADVLR
     ASERKISIDE IQRKVAEHYN IRLSDMIGPK RVRNFARPRQ VAMYLCKQLT SRSLPEIGRR
     FGGRDHTTVM HGVRRIEELR QQDGQIDEDV EMLRRALEA
//
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