ID F6IIN6_9SPHN Unreviewed; 477 AA.
AC F6IIN6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 28-MAR-2018, entry version 48.
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:SAAS00747961}.
CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC ECO:0000256|SAAS:SAAS00555179}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 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:SAAS00747950};
KW Complete proteome {ECO:0000313|Proteomes:UP000009242};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW ECO:0000256|SAAS:SAAS00747973};
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:SAAS00748008};
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
//