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Database: UniProt
Entry: A0A0E3U315_9ENTR
LinkDB: A0A0E3U315_9ENTR
Original site: A0A0E3U315_9ENTR 
ID   A0A0E3U315_9ENTR        Unreviewed;       465 AA.
AC   A0A0E3U315;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   05-JUL-2017, entry version 19.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:AKC59612.1};
GN   ORFNames=BTURN675_016 {ECO:0000313|EMBL:AKC59612.1};
OS   Blochmannia endosymbiont of Polyrhachis (Hedomyrma) turneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=1505596 {ECO:0000313|EMBL:AKC59612.1, ECO:0000313|Proteomes:UP000033094};
RN   [1] {ECO:0000313|EMBL:AKC59612.1, ECO:0000313|Proteomes:UP000033094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=675 {ECO:0000313|EMBL:AKC59612.1};
RX   PubMed=25861561;
RA   Williams L.E., Wernegreen J.J.;
RT   "Genome evolution in an ancient bacteria-ant symbiosis: parallel gene
RT   loss among Blochmannia spanning the origin of the ant tribe
RT   Camponotini.";
RL   PeerJ 3:E881-E881(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}.
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; CP010048; AKC59612.1; -; Genomic_DNA.
DR   RefSeq; WP_046289061.1; NZ_CP010048.1.
DR   EnsemblBacteria; AKC59612; AKC59612; BTURN675_016.
DR   KEGG; bed:BTURN675_016; -.
DR   PATRIC; fig|1505596.4.peg.16; -.
DR   KO; K02313; -.
DR   Proteomes; UP000033094; Chromosome.
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; 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.
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:UP000033094};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033094}.
FT   DOMAIN      162    293       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      373    442       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     170    177       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   465 AA;  53032 MW;  F629623F6E3B5748 CRC64;
     MSFSIWQYCL IFLKKELSAT EFSTWIRPLQ VELISNILTI YAPNRFVLDW IRAKYLSHIS
     SCLNSFCGTN APLLCFKIGK KPLHISDSGK DNIYNSGRSS ILSSIGRSSG FVVWSNSSSQ
     SELFYQSNIN PKHNFNNFLE GKCNQLARAA AQQIVEHNIG GIYNPLFLYG GTGVGKTHLL
     HAVGNGIMMK CSSAKVVYMR SEQFVQDMVQ ALQNNTIEKF KLYYRSVDAL LIDDIQFFAN
     KVRSQEEFFH TLNALLEGNQ QIVLTSDCYP KKIQGLMDRL KSRFAWGLTV GIESPEVEIC
     VRILMQRAEE KNVIFPQDVA LFIAKRLHSN IRELEGAFNC VVANSNFTGK SITVEFVRES
     LKDLFSFRTR IVTVNHIQKI VSEYYRIKIV DLLSKRRSRS LVRPRQIAMA LSKELSNNSL
     SEIGNAFGGR DRTTVLYSCK KIKRLCEENH CIKEDFLHLT NMLFS
//
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