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Database: UniProt
Entry: A0A0N1BSH5_9PROT
LinkDB: A0A0N1BSH5_9PROT
Original site: A0A0N1BSH5_9PROT 
ID   A0A0N1BSH5_9PROT        Unreviewed;       471 AA.
AC   A0A0N1BSH5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   25-OCT-2017, entry version 16.
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=IP70_15025 {ECO:0000313|EMBL:KPF84612.1};
OS   alpha proteobacterium AAP38.
OC   Bacteria; Proteobacteria; Alphaproteobacteria.
OX   NCBI_TaxID=1523418 {ECO:0000313|EMBL:KPF84612.1, ECO:0000313|Proteomes:UP000037884};
RN   [1] {ECO:0000313|EMBL:KPF84612.1, ECO:0000313|Proteomes:UP000037884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP38 {ECO:0000313|EMBL:KPF84612.1,
RC   ECO:0000313|Proteomes:UP000037884};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome
RT   Sequencing.";
RL   Submitted (AUG-2015) 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:KPF84612.1}.
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DR   EMBL; LJHR01000022; KPF84612.1; -; Genomic_DNA.
DR   RefSeq; WP_054168599.1; NZ_LJHR01000022.1.
DR   EnsemblBacteria; KPF84612; KPF84612; IP70_15025.
DR   PATRIC; fig|1523418.3.peg.1158; -.
DR   Proteomes; UP000037884; 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:UP000037884};
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:UP000037884}.
FT   DOMAIN      168    296       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      379    448       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     176    183       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   471 AA;  52816 MW;  A154FD93C7B18AB3 CRC64;
     MSVQGSLDQQ WARVRGRLKD EVGETAYRSW LKPLTVGSLD GGQLRILVPT RFMRDWIRTH
     YADRIRALFS GENPGVQSVE IVVASAAKPD LTATPANDAP VAPPAAKPEP VTELVIEPSP
     ALVVVEDRTD EMSAPLDPRF TFENFVVGKP NELAFAAARR VADAQAVPFN PLFLYGGVGL
     GKTHLMHAIA WAIRKKDPSR RVIYLSAEKF MYQFIRALRF KDTMAFKEQF RSVDVLMIDD
     VQFISGKDST QEEFFHTFNA LVDQNRQVII SADKSPSDLE GMEERLRSRL GWGLVADIHP
     TTYELRLGIL GQKADRIGAK VPPKVLEFLA HKITSNVREL EGALNRIVAH AELVGRAITL
     ESAQDVLHDL LRASNRRVTI EEIQKKVAEH FNIRLADMSS ARRARAVARP RQVAMYLAKQ
     LTQRSLPEIG RKFGDRDHTT VMHAVRKVDE LCGTDPAFAE DVELLRRMLE G
//
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