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Database: UniProt
Entry: F1VVH7_9BURK
LinkDB: F1VVH7_9BURK
Original site: F1VVH7_9BURK 
ID   F1VVH7_9BURK            Unreviewed;       464 AA.
AC   F1VVH7;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   25-OCT-2017, entry version 44.
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=IMCC9480_308 {ECO:0000313|EMBL:EGF33394.1};
OS   Oxalobacteraceae bacterium IMCC9480.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae.
OX   NCBI_TaxID=937450 {ECO:0000313|EMBL:EGF33394.1, ECO:0000313|Proteomes:UP000004494};
RN   [1] {ECO:0000313|EMBL:EGF33394.1, ECO:0000313|Proteomes:UP000004494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC9480 {ECO:0000313|EMBL:EGF33394.1,
RC   ECO:0000313|Proteomes:UP000004494};
RX   PubMed=21572000; DOI=10.1128/JB.05088-11;
RA   Oh H.M., Lee K., Jang Y., Kang I., Kim H.J., Kang T.W., Kim S.Y.,
RA   Cho J.C.;
RT   "Genome sequence of strain IMCC9480, a xanthorhodopsin-bearing
RT   betaproteobacterium isolated from the Arctic Ocean.";
RL   J. Bacteriol. 193:3421-3421(2011).
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:EGF33394.1}.
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DR   EMBL; AEPR01000076; EGF33394.1; -; Genomic_DNA.
DR   RefSeq; WP_009664892.1; NZ_AEPR01000076.1.
DR   EnsemblBacteria; EGF33394; EGF33394; IMCC9480_308.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000004494; 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:UP000004494};
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:UP000004494}.
FT   DOMAIN      161    293       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      372    441       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     169    176       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   464 AA;  52034 MW;  9676F70F81E88D23 CRC64;
     MDNFWQTCSA QLEQELTPQQ FSAWIKPLVP LDYEEGRLRI AAPNRFKLDW VKTQFANRIT
     VLAGQYWEEP IDVQFVLDPR LNAPRKPTAA MPVAARAEGN GINGMSASVG GLIDLPPVDS
     APRRDQSRVN TALTFDSFVT GKANQLARAA AIQVADNPGV SYNPLFLYGG VGLGKTHLVH
     AIGNQVMADN PSAKIRYIHA EQYVRDVVTA YQRKGFDDFK RYYHSLDVLL IDDIQFFGGK
     SRTQEEFFYA FEALIAAKKQ IIITSDTYPK EITGMDDRLI SRFDSGLTVA VEPPELEMRV
     AILLKKAAQE GVNFSDDVAF FVAKHLRSNV RELEGALRKI LAFSRFHGKD ITIEVVKDAL
     KDLLSVQNRQ ISVENIQKTV ADFFNIKVAD MYSKKRPANI ARPRQIAMYL AKELTQKSLP
     EIGELFGGRD HTTVLHAVRK IGADRSKSPE CNHELHVLEQ TLKG
//
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