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Database: UniProt
Entry: A0A0N8PNU6_9BACL
LinkDB: A0A0N8PNU6_9BACL
Original site: A0A0N8PNU6_9BACL 
ID   A0A0N8PNU6_9BACL        Unreviewed;       458 AA.
AC   A0A0N8PNU6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   25-OCT-2017, entry version 15.
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=AN477_17320 {ECO:0000313|EMBL:KPV42509.1};
OS   Alicyclobacillus ferrooxydans.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Alicyclobacillus.
OX   NCBI_TaxID=471514 {ECO:0000313|EMBL:KPV42509.1, ECO:0000313|Proteomes:UP000050482};
RN   [1] {ECO:0000313|EMBL:KPV42509.1, ECO:0000313|Proteomes:UP000050482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC-34 {ECO:0000313|EMBL:KPV42509.1,
RC   ECO:0000313|Proteomes:UP000050482};
RA   Hemp J.;
RT   "Draft genome sequence of Alicyclobacillus ferrooxydans DSM 22381.";
RL   Submitted (SEP-2015) 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:SAAS00911680}.
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:KPV42509.1}.
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DR   EMBL; LJCO01000076; KPV42509.1; -; Genomic_DNA.
DR   RefSeq; WP_054970432.1; NZ_LJCO01000076.1.
DR   EnsemblBacteria; KPV42509; KPV42509; AN477_17320.
DR   PATRIC; fig|471514.4.peg.3591; -.
DR   Proteomes; UP000050482; 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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000050482};
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:UP000050482}.
FT   DOMAIN      153    281       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      365    434       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     161    168       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   458 AA;  51770 MW;  121345329130ED2E CRC64;
     MTNKFDHVFF EQLWSKVLQM MKERMSGPSF ETWFQGTQIT DYNGSTKQLR IFVPTLFACN
     WLVSNYTAIV QNALTALTEQ EFRVEFYTGE KMSGEEDKES AAAVAQPGVD ELPIDMSTSQ
     LNPKYTFDNF VIGQSNRFAH AASLAVAEKP AASYNPLFIY GGVGLGKTHL MQAVGNHVVQ
     FNPGAKVLYL SSERFTNEFI SAIRENKTGD FRNRYRNIDV LLIDDIQFLA NKEQTQEEFF
     HTFNALHEAG RQIVISSDRP PREIPTLEDR LRSRFEWGLI TDIQAPDLET RIAIIQRKAK
     ADGMFLDEHV AYFIATQVSH NIRELEGALI RVVAYSSLVN ADITVDLAEQ ALKDLINQDA
     PRKITVTHIQ KVVGDHYGLK IDELKAKRRT KEVVLPRQIA MYLARELTDM SLPKIGDAFG
     GRDHTTVLHA CERITSSMKT DSALQHTVQK LAEAISTL
//
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