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Database: UniProt
Entry: A0A165RUV9_9SPHN
LinkDB: A0A165RUV9_9SPHN
Original site: A0A165RUV9_9SPHN 
ID   A0A165RUV9_9SPHN        Unreviewed;       486 AA.
AC   A0A165RUV9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   13-FEB-2019, entry version 21.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=A3711_11935 {ECO:0000313|EMBL:KZX54807.1};
OS   Erythrobacter sp. HI00D59.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter.
OX   NCBI_TaxID=1822215 {ECO:0000313|EMBL:KZX54807.1, ECO:0000313|Proteomes:UP000077319};
RN   [1] {ECO:0000313|EMBL:KZX54807.1, ECO:0000313|Proteomes:UP000077319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI00D59 {ECO:0000313|EMBL:KZX54807.1,
RC   ECO:0000313|Proteomes:UP000077319};
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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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:KZX54807.1}.
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DR   EMBL; LWEG01000010; KZX54807.1; -; Genomic_DNA.
DR   RefSeq; WP_067671646.1; NZ_LWEG01000010.1.
DR   EnsemblBacteria; KZX54807; KZX54807; A3711_11935.
DR   Proteomes; UP000077319; 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   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:SAAS00756129};
KW   Complete proteome {ECO:0000313|Proteomes:UP000077319};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077319}.
FT   DOMAIN      182    310       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      394    463       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     190    197       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   486 AA;  54413 MW;  98D1ACC6CE9252D3 CRC64;
     MRKTSDIGAK KAQDDFMEDQ DAVNLAADWA DISQGLRKDL GHQLHSQWIK PIQVGGIDRD
     TGTLDLFLPT EFSANWVKDR FADRLSLAWK IARSEVRDVR IQVHPGRRQV ADLRLHADGR
     RPANDGADNS MMAISADTLG DAGFTSSVGL DPSLTFAAFI TGEANVLAFN AAQRIGATEK
     PQFSPLYLKA ATGQGKTHLL HAIGHSFLQA HPRSRIFYCS AERFMVEFVQ ALKANQMLEF
     KARLRSFDLL LVDDIQFIIG KASAQEELLY TIDALLAEGK RLVFAADRAP QALDGVEPRL
     LSRLSMGLVA DIQAADIELR KKILTSKLTR FAPLEVPADV LDFLARTITR NIRELVGGLN
     KLIAYAQLTG QEVSLQLAEE QLTDILSANR RRITIDEIQR TVCQFYRIDR SEMSSKRRAR
     AVVRPRQVAM YLSKVLTPRS YPEIGRKFGG RDHSTVIHAV RLIEDLRQRD ADMDGDVRSL
     LRQLES
//
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