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Database: UniProt
Entry: A0A0A1F3M9_9BURK
LinkDB: A0A0A1F3M9_9BURK
Original site: A0A0A1F3M9_9BURK 
ID   A0A0A1F3M9_9BURK        Unreviewed;       482 AA.
AC   A0A0A1F3M9;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   22-NOV-2017, entry version 26.
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:AIY39161.1};
GN   ORFNames=LT85_0001 {ECO:0000313|EMBL:AIY39161.1};
OS   Collimonas arenae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Collimonas.
OX   NCBI_TaxID=279058 {ECO:0000313|EMBL:AIY39161.1, ECO:0000313|Proteomes:UP000030302};
RN   [1] {ECO:0000313|EMBL:AIY39161.1, ECO:0000313|Proteomes:UP000030302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cal35 {ECO:0000313|EMBL:AIY39161.1,
RC   ECO:0000313|Proteomes:UP000030302};
RA   Uroz S., Tech J.J., Sawaya N.A., Frey-Klett P., Leveau J.H.J.;
RT   "Structure and function of bacterial communities in ageing soils:
RT   insights from the Mendocino ecological staircase.";
RL   Soil Biol. Biochem. 69:265-274(2014).
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; CP009962; AIY39161.1; -; Genomic_DNA.
DR   RefSeq; WP_038483785.1; NZ_CP009962.1.
DR   EnsemblBacteria; AIY39161; AIY39161; LT85_0001.
DR   KEGG; care:LT85_0001; -.
DR   KO; K02313; -.
DR   Proteomes; UP000030302; 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:UP000030302};
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:UP000030302}.
FT   DOMAIN      179    310       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      390    459       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     187    194       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   482 AA;  53862 MW;  22054C73CBCCD2A1 CRC64;
     MENFWQSCST QLEQELTPQQ FSAWIKPLTP LDYEDGRLRI AAPNRFKLDW VKTQFASRIT
     TLAHQYWEAP IEVLFVLDPR KSTAAPASAI SSMPVALTNN SSNGSEQSGA QASAASGGNY
     GNSNFDRLPE VQTENSAVSA RRDQSRINTA LSFDSFVTGK ANQLARAAAI QVANNPGVSY
     NPLFLYGGVG LGKTHLIHAI GNQLLADNPN AKIRYIHAEQ YVRDVVTAYQ RKGFDDFKRY
     YHSLDLLLID DIQFFGGKSR TQEEFFYAFE ALIAAKKQII ITSDTYPKEI TGMDDRLISR
     FDSGLTVAIE PPELEMRVAI LLKKAASEGV TFSDDVAFFV AKHLRSNVRE LEGALRKILA
     YSRFHGKDIS IDVVKDALKD LLSVQNRQIS VENIQKTVAD FFNIKVADMY SKKRPANIAR
     PRQIAMYLAK ELTQKSLPEI GELFGGRDHT TVLHAVRKIA GDRTKNPECN HELHVLEQTL
     KG
//
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