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Database: UniProt
Entry: Q1NGR2_SPHSS
LinkDB: Q1NGR2_SPHSS
Original site: Q1NGR2_SPHSS 
ID   Q1NGR2_SPHSS            Unreviewed;       466 AA.
AC   Q1NGR2;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   16-JAN-2019, entry version 79.
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=SKA58_05030 {ECO:0000313|EMBL:EAT09793.1};
OS   Sphingomonas sp. (strain SKA58).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=314266 {ECO:0000313|EMBL:EAT09793.1, ECO:0000313|Proteomes:UP000005395};
RN   [1] {ECO:0000313|EMBL:EAT09793.1, ECO:0000313|Proteomes:UP000005395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKA58 {ECO:0000313|EMBL:EAT09793.1,
RC   ECO:0000313|Proteomes:UP000005395};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.C.;
RL   Submitted (MAR-2006) 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:EAT09793.1}.
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DR   EMBL; AAQG01000002; EAT09793.1; -; Genomic_DNA.
DR   RefSeq; WP_009820782.1; NZ_CH959306.1.
DR   ProteinModelPortal; Q1NGR2; -.
DR   STRING; 314266.SKA58_05030; -.
DR   EnsemblBacteria; EAT09793; EAT09793; SKA58_05030.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   Proteomes; UP000005395; 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:SAAS00756129};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005395};
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}.
FT   DOMAIN      162    296       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      374    443       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     170    177       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   466 AA;  51316 MW;  731290FBB966B22D CRC64;
     MKVGAALVER QATDSENGTG LDSAWSVIRT GLRRDVGARL FDQWLKPARL GDYCPESQTL
     DLLVATDFSA NFVSGQFGDR LRMAWRSAGV GVREVRVRRA PDACGPRLLE VAPSIQTEPV
     MEEAIVASNF QPRHRLDDFV VGDTNRLAWS AAQAMAGEAQ PRFTPLFIHG GTGQGKTHLL
     HGIAAAFSAH SPKAPVLYMS AERFMMEFVN AMRANETMAF KARLRAARLL LIDDIQFIAG
     KGSTQEEFLH TINDLIDSGA RIVVTADRAP QMLESIDARI LSRLAGGLVA DIRPADLDLR
     LAILESKRAL AGDMIVPDMV IDFLARSIRS NVRELEGAFN KLVAYGQLTG RAVDLDFAQQ
     MLADAVRANA RRITVDEIQK ACAAHFKIDP AEMRSKRRAR AVARPRQVAM YLAKKMTPRS
     LPEIGRIFGG RDHSTVIHAV RTIEALRETS PDMDADVRAL QRLLEG
//
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