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Database: UniProt
Entry: H8KZ21_FRAAD
LinkDB: H8KZ21_FRAAD
Original site: H8KZ21_FRAAD 
ID   H8KZ21_FRAAD            Unreviewed;       461 AA.
AC   H8KZ21;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   05-JUL-2017, entry version 41.
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   OrderedLocusNames=Fraau_0001 {ECO:0000313|EMBL:AFC84512.1};
OS   Frateuria aurantia (strain ATCC 33424 / DSM 6220 / NBRC 3245 / NCIMB
OS   13370) (Acetobacter aurantius).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Frateuria.
OX   NCBI_TaxID=767434 {ECO:0000313|EMBL:AFC84512.1, ECO:0000313|Proteomes:UP000005234};
RN   [1] {ECO:0000313|Proteomes:UP000005234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33424 / DSM 6220 / NBRC 3245 / NCIMB 13370
RC   {ECO:0000313|Proteomes:UP000005234};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G.,
RA   Teshima H., Kyrpides N., Mavromatis K., Ivanova N., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Frateuria aurantia DSM 6220.";
RL   Submitted (FEB-2012) 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}.
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DR   EMBL; CP003350; AFC84512.1; -; Genomic_DNA.
DR   RefSeq; WP_014401518.1; NC_017033.1.
DR   EnsemblBacteria; AFC84512; AFC84512; Fraau_0001.
DR   KEGG; fau:Fraau_0001; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000005234; Chromosome.
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:UP000005234};
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:UP000005234}.
FT   DOMAIN      158    388       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      369    438       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     166    173       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   461 AA;  52356 MW;  68B4FC7FEA20EB3F CRC64;
     MSDLWRRCLL RLETELSAEE LHTWLMPLQA RDDPEGLRLF APNPYTLDTV SERYLALITR
     VISQLTGHDL KVKLEVGSNT PMARPSSRPS LSARAGGHPD EVLRQEVIQP SHAVPERTEA
     SFAHNLNLHY TFDTFVEGKS NQLGKAAAMQ VAMNPGKAYN PLLLYGGTGL GKTHLMHAAG
     NLMLERNPDF KVLYLRSEQF VGSMIEALRT KSMDEFKRRF RSVDALLIDD IQFFAGKDTT
     QEEFFHTFNA LFESKQQIVL TCDRYPKEVD KLEPRLKSRL GWGLSVAIEP PDFETRAAIL
     LAKAQEKDVV MSDEVAMLLA KRIRSNVRDL EGALNTLAAR ANFYGRPITV EFAEETLRDL
     LATHAQAITI PNIQKITADY YQVRLQDLLS KRRVRSLARP RQIAMSLSKE LTEHSLPEIG
     EAFGGRDHTT VLHACRTIRK FCETDNRMRQ DWEQLIRILT G
//
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