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Database: UniProt
Entry: A0A0X8R0Q9_9SPHN
LinkDB: A0A0X8R0Q9_9SPHN
Original site: A0A0X8R0Q9_9SPHN 
ID   A0A0X8R0Q9_9SPHN        Unreviewed;       453 AA.
AC   A0A0X8R0Q9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   25-OCT-2017, entry version 14.
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   ECO:0000313|EMBL:AMG73124.1};
GN   ORFNames=SGRAN_0729 {ECO:0000313|EMBL:AMG73124.1};
OS   Sphingopyxis granuli.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=267128 {ECO:0000313|EMBL:AMG73124.1, ECO:0000313|Proteomes:UP000058599};
RN   [1] {ECO:0000313|EMBL:AMG73124.1, ECO:0000313|Proteomes:UP000058599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TFA {ECO:0000313|EMBL:AMG73124.1,
RC   ECO:0000313|Proteomes:UP000058599};
RX   PubMed=26847793; DOI=10.1186/s12864-016-2411-1;
RA   Garcia-Romero I., Perez-Pulido A.J., Gonzalez-Flores Y.E.,
RA   Reyes-Ramirez F., Santero E., Floriano B.;
RT   "Genomic analysis of the nitrate-respiring Sphingopyxis granuli
RT   (formerly Sphingomonas macrogoltabida) strain TFA.";
RL   BMC Genomics 17:93-93(2016).
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; CP012199; AMG73124.1; -; Genomic_DNA.
DR   EnsemblBacteria; AMG73124; AMG73124; SGRAN_0729.
DR   KEGG; sgi:SGRAN_0729; -.
DR   PATRIC; fig|267128.3.peg.777; -.
DR   KO; K02313; -.
DR   Proteomes; UP000058599; 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:UP000058599};
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:UP000058599}.
FT   DOMAIN      149    283       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      361    430       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     157    164       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   453 AA;  50006 MW;  492396F5868FD2FB CRC64;
     MSGDAAALWP RVAEGLRRDL GARTFDHWLK PVRFADYCTL SAVVTLETAS RFSANWINDR
     FGERLLLAWR QYLPAVRSVT VRGGAAASDR AATLATAPLP AFDATPVPAV QTVPSPFDAR
     LCFDRFVVAR SNILAANAAR RMAMAEAPQF NPLYLCSGTG QGKTHLLHAI AQAYAAIRPT
     ANIILMSAEK FMLEFVGAMR GGDMMAFKAR LRAADLLLLD DLQFVIGKNS TQEELLHTID
     DLMCSGKRLV VTADRPPAML DGVEARLLSR LSGGLVADIE APEDDLRERI IRQRLAAMPM
     VAVPDDVVAY LVRHFTRNIR ELEGALNKLL AYAALTGVDV DLALAEDRLA ENVRSARPRI
     TIDEIQRAVC AHYRLDKAEM ASKRRVRAIA RPRQVAMYLA KELTPRSYPE IGRRFGGRDH
     STVIHAVRTV EALRVTDSEL DAEIAAIRRS LNN
//
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