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Database: UniProt
Entry: F7WYV4_9GAMM
LinkDB: F7WYV4_9GAMM
Original site: F7WYV4_9GAMM 
ID   F7WYV4_9GAMM            Unreviewed;       449 AA.
AC   F7WYV4;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-SEP-2017, entry version 44.
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:AEH39604.1};
GN   ORFNames=BCTU_004 {ECO:0000313|EMBL:AEH39604.1};
OS   Buchnera aphidicola (Cinara tujafilina).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=261317 {ECO:0000313|EMBL:AEH39604.1, ECO:0000313|Proteomes:UP000006811};
RN   [1] {ECO:0000313|EMBL:AEH39604.1, ECO:0000313|Proteomes:UP000006811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21571878; DOI=10.1128/AEM.00141-11;
RA   Lamelas A., Gosalbes M.J., Moya A., Latorre A.;
RT   "The genome of Buchnera aphidicola from the aphid Cinara tujafilina
RT   provides new clues about the evolutionary history of metabolic losses
RT   in bacterial endosymbionts.";
RL   Appl. Environ. Microbiol. 0:0-0(2011).
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}.
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DR   EMBL; CP001817; AEH39604.1; -; Genomic_DNA.
DR   STRING; 261317.BCTU_004; -.
DR   EnsemblBacteria; AEH39604; AEH39604; BCTU_004.
DR   KEGG; baj:BCTU_004; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000006811; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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:UP000006811};
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006811};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     37     59       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      155    284       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      366    435       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     163    170       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   449 AA;  52756 MW;  C831CE5148144DDB CRC64;
     MSLAIWKKCL THLQKKLLPT EFSMWIRPLR VKSKKILYIY LHQIILSWIG LKTSIYTILK
     IYYINLVKKK NIPLTLQIEN ISTDHLITTH TYYSKYNIIN QQKIHKKHFN YNIHYIKSYY
     HTEINKKYCF NNFIEGESNR LARYSSYQLA KLKNSYNPLF LYGNTGLGKT HLLHAIGNFI
     LENNNTAKVI YIHSERFCAN MVKSIKNNSI EEFKKYYRSV DALMIDDIQF FSNKERSQEE
     LFHTFNTLFD HDQKIILTSD RYPKDINGMA DRLKSRFSWG LTISINPPDL NTRIAILLYK
     AAERKIKLSY TIAQFIATKL CSNVRELEGI LNKLQNHSIF NQKNINIELV QSTLQDLLIC
     QKEKITIKNI QKSVSKYFSI KMSDMLSKKR TRSIAQPRQI AMALVKKLTN HSLSEIGIAF
     GGKDHTTVLH ACRKIKELSK KIKKFIMIF
//
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