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Database: UniProt
Entry: A0A060USN7_9PROT
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ID   A0A060USN7_9PROT        Unreviewed;       452 AA.
AC   A0A060USN7;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   05-JUL-2017, entry version 26.
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:CDQ09808.1};
GN   ORFNames=AFERRI_30454 {ECO:0000313|EMBL:CDQ09808.1};
OS   Acidithiobacillus ferrivorans.
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=160808 {ECO:0000313|EMBL:CDQ09808.1, ECO:0000313|Proteomes:UP000029069};
RN   [1] {ECO:0000313|EMBL:CDQ09808.1, ECO:0000313|Proteomes:UP000029069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF27 {ECO:0000313|EMBL:CDQ09808.1,
RC   ECO:0000313|Proteomes:UP000029069};
RA   Genoscope - CEA;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDQ09808.1, ECO:0000313|Proteomes:UP000029069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF27 {ECO:0000313|EMBL:CDQ09808.1,
RC   ECO:0000313|Proteomes:UP000029069};
RA   Talla E., Hedrich S., Mangenot S., Ji B., Johnson D.B., Barbe V.,
RA   Bonnefoy V.;
RT   "Initial genome analysis of the psychrotolerant acidophile
RT   Acidithiobacillus ferrivorans CF27: insights into iron and sulfur
RT   oxidation pathways and into biofilm formation.";
RL   Submitted (JUL-2014) 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}.
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:CDQ09808.1}.
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DR   EMBL; CCCS020000023; CDQ09808.1; -; Genomic_DNA.
DR   RefSeq; WP_035192039.1; NZ_LT841305.1.
DR   STRING; 743299.Acife_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   Proteomes; UP000029069; Unassembled WGS sequence.
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:UP000029069};
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}.
FT   DOMAIN      149    362       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      360    429       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     157    164       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   452 AA;  51001 MW;  13A17C81D6524A1D CRC64;
     MSSHPAPSAL RNGDALWAAL CVQLQEQTTA QQFNTWLRPL RGELHGNELH LFAPNTFVME
     WVRERLIDLL EAVLGELAPG MMLRLELSTD GAAALAPVVA ATPATTSITD PRNGNRLNPG
     FSFKSYVAGK SNQLAVAAAL QVAKNPGKSY NPLYIYGGVG LGKTHLMQAV GNAILQRDAN
     AKVLYVTSEG FIMDMVRSLQ HNTINDFKQR YRKLDALLID DIQFFAGKDR TQEEFFHTFN
     ALFDGGRQII ITCDRYPKEV DRLEERLQSR FGWGLTVAIQ PHDLETRMAI VLCKAEESGI
     DLPEEVAFFI AEKIRSHVRE LEGALRRIIA HVNFTHKPYN LDTAREALRD LIDVQKRMVS
     LDNIQKVVAE YFHIRGSDMQ SKRRSRNIAR PRQVAMCLTK ELTNHSLPEI GEAFGGRDHT
     TVLHACRQID KLRQEDTQMD EDYRNLLRIL GA
//
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