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Database: UniProt
Entry: A0A167J1Y0_9SPHN
LinkDB: A0A167J1Y0_9SPHN
Original site: A0A167J1Y0_9SPHN 
ID   A0A167J1Y0_9SPHN        Unreviewed;       492 AA.
AC   A0A167J1Y0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   05-JUL-2017, entry version 11.
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=A3736_07990 {ECO:0000313|EMBL:KZY56514.1};
OS   Erythrobacter sp. HI0063.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter.
OX   NCBI_TaxID=1822240 {ECO:0000313|EMBL:KZY56514.1, ECO:0000313|Proteomes:UP000077326};
RN   [1] {ECO:0000313|EMBL:KZY56514.1, ECO:0000313|Proteomes:UP000077326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI0063 {ECO:0000313|EMBL:KZY56514.1,
RC   ECO:0000313|Proteomes:UP000077326};
RA   Sosa O.A.;
RT   "Microbial cycling of marine high molecular weight dissolved organic
RT   matter.";
RL   Submitted (MAR-2016) 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:SAAS00756131}.
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:KZY56514.1}.
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DR   EMBL; LWFF01000214; KZY56514.1; -; Genomic_DNA.
DR   RefSeq; WP_067680977.1; NZ_LWFF01000214.1.
DR   EnsemblBacteria; KZY56514; KZY56514; A3736_07990.
DR   Proteomes; UP000077326; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
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:SF12; PTHR30050:SF12; 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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000077326};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077326}.
FT   DOMAIN      188    316       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      400    469       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     196    203       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   492 AA;  54955 MW;  37F31D8D1D568151 CRC64;
     MGRTSGGAQE RQPERQKGRD DLMEDLEAIN LAADWADISQ GLRKDLGHQL HSQWIKPIQI
     GGIDRETGTL DLFLPTEFSA KWVQDRFADR LSLAWKIASA EVRNVRISVH PGRRKVADPH
     LHSDGRRAAN DGADTGMMAI AADTIGDAGF TSHVGLDASL TFAAFVTGEA NVLACNAAQR
     MAAPEQPQFS PLYLKAGTGQ GKTHLLHAIG HSFLKSHPRS RIFYCSAERF MVEFVQALKQ
     NQMMEFKARL RSFDLLLVDD IQFIIGKASA QEELLYTIDA LLAEGKRLVF AADRAPQALD
     GVEPRLLSRL SMGLVADIQP ADIELRKTIL ESKLTKFAPL EVPGDVIEFL ARTITRNVRE
     LVGGLNKLIA YAQLTGQEVS LQLAEEQLTD ILSANRRRIT IDEIQRTVCQ FYRIDRSEMS
     SKRRARAVVR PRQVAMYLSK VLTPRSYPEI GRKFGGRDHS TVIHAVRLIE DLRQRDADMD
     GDVRSLLRQL ES
//
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