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Database: UniProt
Entry: A0A0N1B8Z6_9PROT
LinkDB: A0A0N1B8Z6_9PROT
Original site: A0A0N1B8Z6_9PROT 
ID   A0A0N1B8Z6_9PROT        Unreviewed;       488 AA.
AC   A0A0N1B8Z6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   25-OCT-2017, entry version 16.
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=IP84_03485 {ECO:0000313|EMBL:KPF70109.1};
OS   beta proteobacterium AAP99.
OC   Bacteria; Proteobacteria; Betaproteobacteria.
OX   NCBI_TaxID=1523428 {ECO:0000313|EMBL:KPF70109.1, ECO:0000313|Proteomes:UP000037960};
RN   [1] {ECO:0000313|EMBL:KPF70109.1, ECO:0000313|Proteomes:UP000037960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP99 {ECO:0000313|EMBL:KPF70109.1,
RC   ECO:0000313|Proteomes:UP000037960};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome
RT   Sequencing.";
RL   Submitted (AUG-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:KPF70109.1}.
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DR   EMBL; LJIA01000002; KPF70109.1; -; Genomic_DNA.
DR   RefSeq; WP_054124523.1; NZ_LJIA01000002.1.
DR   EnsemblBacteria; KPF70109; KPF70109; IP84_03485.
DR   PATRIC; fig|1523428.3.peg.1779; -.
DR   Proteomes; UP000037960; 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:UP000037960};
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:UP000037960}.
FT   DOMAIN      185    316       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      396    465       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     193    200       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   488 AA;  53919 MW;  CE08B930E3183C29 CRC64;
     MDSASHAGDH FWARCCERLG NQLTREQFVA WVKPISAGAY DADARRLTLL APNRAKAEHF
     RGEYLREVQS WTEELFGYRV DLNLEIGSPA AGSGTPASQP SAHGAGIETS GGPAPLASLL
     QGAAESAAAA NSNSGASVPP AAAMIDVQER TRVNTVLRFD NFVSGKANQL ARAAALQVAD
     NPGVSYNPFF LYGGTGLGKT HLIHAIGNAM LDAKPDARVR YIHAEQYVAD VVRAYQRKDF
     DAFKRYYHSL DLLLIDDIQF FAGKERTQEE FFYLFEALTA AKSQIIITSD TYPKELSDID
     ERLKSRFDAG LTVAIEPPEL EMRVAILQQK AEELGKLLES EVAFFIAKHL RSNVRELEGA
     LKKVVAYCDF HGKTITLDTA KDALRDLLQV SRGQISIEVI QKTVADYYKI KVADMYSKRR
     PANIAVPRQV AMYLAKELTQ KSLPEIGELF GGRDHTTVLH AVRKIGTERG KDVQLNHTLH
     VLEQTLKS
//
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