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Database: UniProt
Entry: G2KR69_MICAA
LinkDB: G2KR69_MICAA
Original site: G2KR69_MICAA 
ID   G2KR69_MICAA            Unreviewed;       471 AA.
AC   G2KR69;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   25-OCT-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:AEP08721.1};
GN   OrderedLocusNames=MICA_376 {ECO:0000313|EMBL:AEP08721.1};
OS   Micavibrio aeruginosavorus (strain ARL-13).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Micavibrio.
OX   NCBI_TaxID=856793 {ECO:0000313|EMBL:AEP08721.1, ECO:0000313|Proteomes:UP000009286};
RN   [1] {ECO:0000313|EMBL:AEP08721.1, ECO:0000313|Proteomes:UP000009286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARL-13 {ECO:0000313|EMBL:AEP08721.1,
RC   ECO:0000313|Proteomes:UP000009286};
RX   PubMed=21936919; DOI=10.1186/1471-2164-12-453;
RA   Wang Z., Kadouri D., Wu M.;
RT   "Genomic insights into an obligate epibiotic bacterial predator:
RT   Micavibrio aeruginosavorus ARL-13.";
RL   BMC Genomics 12:453-453(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: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; CP002382; AEP08721.1; -; Genomic_DNA.
DR   RefSeq; WP_014101944.1; NC_016026.1.
DR   STRING; 856793.MICA_376; -.
DR   EnsemblBacteria; AEP08721; AEP08721; MICA_376.
DR   KEGG; mai:MICA_376; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000009286; 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:UP000009286};
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:UP000009286}.
FT   DOMAIN      168    296       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      379    448       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     176    183       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   471 AA;  53256 MW;  F0F9D3BB9A4DE965 CRC64;
     MKSNEVLSFK NDSFKPTPEI LDLWNTIHNA LRGEFGEAVF RSWLKPLTLQ AYYHGTLEVS
     VPTRFMRDWI QSHYSARILE MCAGVNADVR RLEIVVVQSG ARPAEDEQVA AAPAPVAPVK
     SNQNEEEDPF GLSAPFDPRF TFDTFVVGKP NALAHAAARR IVESPNVPFN PLFLYGGVGL
     GKTHLMHAIG QAMKDKWPNR RVVYLSAEKF MYQFVRALRA KDTMAFKEAF RSVDVLMIDD
     IQFISGKEST QEEFFHTFNA LVDQNKQIVI SADKAPSDLT GLEERLRSRL AWGLVADIHP
     STYDLRLGIL QSKREQLGAE IPDAVLEFLA LKVTSNIREL EGALNRIVAH ADVTKQPVTL
     ESTQDVLQDL LRAHDRRITI DEIQRKVAEH YNIRLPDMHS ARRARNVARP RQVAMYLAKQ
     LTSRSLPEIG RKFGGRDHTT VMHAVRKIEE LMVEDAQIAQ DVDVIRRSLT G
//
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