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Database: UniProt
Entry: A0A0F7JZN1_9GAMM
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ID   A0A0F7JZN1_9GAMM        Unreviewed;       453 AA.
AC   A0A0F7JZN1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   25-OCT-2017, entry version 19.
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:AKH21107.1};
GN   ORFNames=AAY24_12910 {ECO:0000313|EMBL:AKH21107.1};
OS   Sedimenticola thiotaurini.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Sedimenticola.
OX   NCBI_TaxID=1543721 {ECO:0000313|EMBL:AKH21107.1, ECO:0000313|Proteomes:UP000034410};
RN   [1] {ECO:0000313|EMBL:AKH21107.1, ECO:0000313|Proteomes:UP000034410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIP-G1 {ECO:0000313|EMBL:AKH21107.1,
RC   ECO:0000313|Proteomes:UP000034410};
RX   PubMed=26089430;
RA   Flood B.E., Jones D.S., Bailey J.V.;
RT   "Complete Genome Sequence of Sedimenticola thiotaurini Strain SIP-G1,
RT   a Polyphosphate- and Polyhydroxyalkanoate-Accumulating Sulfur-
RT   Oxidizing Gammaproteobacterium Isolated from Salt Marsh Sediments.";
RL   Genome Announc. 3:e00671-15(2015).
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; CP011412; AKH21107.1; -; Genomic_DNA.
DR   RefSeq; WP_046860036.1; NZ_CP011412.1.
DR   EnsemblBacteria; AKH21107; AKH21107; AAY24_12910.
DR   KEGG; seds:AAY24_12910; -.
DR   PATRIC; fig|1543721.4.peg.2668; -.
DR   KO; K02313; -.
DR   Proteomes; UP000034410; 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:UP000034410};
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:UP000034410}.
FT   DOMAIN      149    305       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;  51254 MW;  89D7E4E9678BD15F CRC64;
     MNFWSKCIDH LEHDLPQQQF NTWIRPLQSV EEAHNIRLLA PNQFVLNWVQ NHYLDNITSY
     LQTIAGSNAP TVSLEIGSRA NTRNSQEQPT GSPISSQDKP RARAPRPEND APMPSNLNPN
     FVFDTFVQGK SNQLARAASI QIGENPGTAY NPLFIYGGVG LGKTHLMHAI GNMILDNNPK
     ARVVYVHSEG FVAQMVKALQ HNTIDDFKRR FRSVNALLID DVQFFAGKER SQEEFFHTFN
     ALFESQQQII LSSDRFPKEV SGLEERLKSR FGWGLTVAIE PPDLETRVAI LKSKADQLFG
     VDLPNEVAFF IGKRVRSNIR ELEGALRRII ANAEFTGRPI TQEFAKDALR DMLAAQDKQV
     TIENIQKTVA EYFKIRTSDL LSSKRSRTIA RPRQIAMSLA KELTNHSLPE IGEAFGGRDH
     TTVLYATRKI LELKESDHRV EEDYGNLLRT LTS
//
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