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Database: UniProt
Entry: A0A0H0XR90_9SPHN
LinkDB: A0A0H0XR90_9SPHN
Original site: A0A0H0XR90_9SPHN 
ID   A0A0H0XR90_9SPHN        Unreviewed;       486 AA.
AC   A0A0H0XR90;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   16-JAN-2019, entry version 25.
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=AAV99_02330 {ECO:0000313|EMBL:KLI64457.1};
OS   Erythrobacter marinus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter.
OX   NCBI_TaxID=874156 {ECO:0000313|EMBL:KLI64457.1, ECO:0000313|Proteomes:UP000053455};
RN   [1] {ECO:0000313|EMBL:KLI64457.1, ECO:0000313|Proteomes:UP000053455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HWDM-33 {ECO:0000313|EMBL:KLI64457.1,
RC   ECO:0000313|Proteomes:UP000053455};
RA   Zhuang L., Liu Y., Shao Z.;
RT   "The draft genome sequence of Erythrobacter marinus HWDM-33.";
RL   Submitted (APR-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: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:KLI64457.1}.
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DR   EMBL; LBHU01000001; KLI64457.1; -; Genomic_DNA.
DR   RefSeq; WP_047092321.1; NZ_LDCP01000001.1.
DR   EnsemblBacteria; KLI64457; KLI64457; AAV99_02330.
DR   PATRIC; fig|874156.12.peg.486; -.
DR   OrthoDB; 219876at2; -.
DR   Proteomes; UP000053455; 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; 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; 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:UP000053455};
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:UP000053455}.
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;  54479 MW;  975085CCEE890E50 CRC64;
     MGQHVTRKCA VKKNGTEGSM EDQQAADLAA DWSDICQGLR KDLGHQLFTQ WVKPIQLGKL
     NQDNGTLDLF LPTEFSANWV KDRYHDRLSL AWKIASSEVR HISIQVHPGR RKIADFDLRG
     QDGFGHRAAN DATMAMESIG DDGFTSSVGL DPTQTFAAFV TGTGNVLAKN AAERMSKAEK
     PQFSPLYLKA ATGQGKTHLM HAIGHSYLQA FPRARIFYCS AERFMVEFVQ ALKSNEMIEF
     KGRLRAFDLL LVDDIQFIIG KAAAQEELLY TIDALLAEGK RLVFAADRAP QALDGVEPRL
     LSRLSMGLVA DIQPADIELR RAILESKLTR FAPLEVPADV IDFLARTVSR NVRELVGGLN
     KLIAYAQLTG QEVSLQLAEE QLTDILSANR RRITIDEIQR TVCQFYRIDR SEMSSKRRAR
     AVVRPRQVAM YLAKVLTPRS YPEIGRKFGG RDHSTVIHAV RLIEDLRTRD ADMDGDVRSL
     LRQLES
//
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