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Database: UniProt
Entry: F6IIN6_9SPHN
LinkDB: F6IIN6_9SPHN
Original site: F6IIN6_9SPHN 
ID   F6IIN6_9SPHN            Unreviewed;       477 AA.
AC   F6IIN6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   25-OCT-2017, entry version 46.
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=PP1Y_AT33855 {ECO:0000313|EMBL:CCA94104.1};
OS   Novosphingobium sp. PP1Y.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=702113 {ECO:0000313|EMBL:CCA94104.1, ECO:0000313|Proteomes:UP000009242};
RN   [1] {ECO:0000313|EMBL:CCA94104.1, ECO:0000313|Proteomes:UP000009242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PP1Y {ECO:0000313|EMBL:CCA94104.1};
RX   PubMed=21685292; DOI=10.1128/JB.05349-11;
RA   D'Argenio V., Petrillo M., Cantiello P., Naso B., Cozzuto L.,
RA   Notomista E., Paolella G., Di Donato A., Salvatore F.;
RT   "De novo sequencing and assembly of the whole genome of
RT   Novosphingobium sp. strain PP1Y.";
RL   J. Bacteriol. 193:4296-4296(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}.
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DR   EMBL; FR856862; CCA94104.1; -; Genomic_DNA.
DR   RefSeq; WP_013834275.1; NC_015580.1.
DR   STRING; 702113.PP1Y_AT33855; -.
DR   EnsemblBacteria; CCA94104; CCA94104; PP1Y_AT33855.
DR   KEGG; npp:PP1Y_AT33855; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000009242; Chromosome.
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:UP000009242};
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:UP000009242}.
FT   DOMAIN      173    301       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      385    454       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     181    188       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   477 AA;  53191 MW;  F8E0A62A0EC3A0F9 CRC64;
     MEEDQEAVNL AADWADISQG LRKDLGHQAH SQWIKPIQPG NYCKETGTLD LYLPTEFSAN
     WVNDRFADRL SLAWKIARPD VRHVRILVHP GRRQLPELRL GHGGRPSHAP ANDSVVGASD
     AISAALNGDA FASLGQGPAG IDASQTFSTF VTGTANVLAC NAAQRMAAGE KPQFSPLYLK
     AATGQGKTHL LHAIGHAYLA NHPHARIFYC SAERFMVEFV QALRQNQMIE FKARLRGFDL
     LLVDDIQFII GKASAQEELL YTIDALLQEG KRLVFAADRA PQALDGVEPR LLSRLSMGLV
     ADIQPADIEL RRSILENRLQ RFASIDVPAD VIEFLARTIN RNVRELVGGL NKLIAYAQLT
     GQAVSLQLAE EQLTDILSAN RRRITIDEIQ RTVCQFYRID RTEMSSKRRA RAVVRPRQVA
     MYLAKVLTPR SYPEIGRKFG GRDHSTVIHA VRLIEELRTR DADMDGDVRS LLRQLES
//
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