GenomeNet

Database: UniProt
Entry: E8RMU2_ASTEC
LinkDB: E8RMU2_ASTEC
Original site: E8RMU2_ASTEC 
ID   E8RMU2_ASTEC            Unreviewed;       473 AA.
AC   E8RMU2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   25-OCT-2017, entry version 53.
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   OrderedLocusNames=Astex_0001 {ECO:0000313|EMBL:ADU11705.1};
OS   Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / VKM B-1370 /
OS   CB 48).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=573065 {ECO:0000313|EMBL:ADU11705.1, ECO:0000313|Proteomes:UP000001492};
RN   [1] {ECO:0000313|Proteomes:UP000001492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15261 / DSM 4724 / VKM B-1370 / CB 48
RC   {ECO:0000313|Proteomes:UP000001492};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brun Y.V., Woyke T.;
RT   "Complete sequence of chromosome 1 of Asticcacaulis excentricus CB
RT   48.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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:SAAS00735475}.
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002395; ADU11705.1; -; Genomic_DNA.
DR   RefSeq; WP_013477539.1; NC_014816.1.
DR   ProteinModelPortal; E8RMU2; -.
DR   STRING; 573065.Astex_0001; -.
DR   EnsemblBacteria; ADU11705; ADU11705; Astex_0001.
DR   KEGG; aex:Astex_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235660; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000001492; Chromosome 1.
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; 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   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:UP000001492};
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:UP000001492}.
FT   DOMAIN      163    291       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      381    450       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     171    178       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   473 AA;  52835 MW;  17A46FFFB5DC1EAE CRC64;
     MPGVNNWSPI QPEMVWTKVA SALRHELGEG PYNSYVAPSA LRQNPLGDPV LVTPTLYARD
     WFARNALRRA NELWAQHDPD HRSLELKSRA EFDDQSKSAP MTPVTRTDSA ENAPAAPVVS
     FQDAVARVAG LQERLTFETF VPGRGNEFAY TMSRQVATWA DGHFNPVFFH GPYGYGKTHL
     LNAIAWEAKA RRQDAKVVYL TAEKFTSTFV KSLQDRSTAA FKDELRSADL LLIDDVHFIG
     GKTSSQEELF HTLTALLENN KRVVFTADRP PSHLNEIEAR LRSHLSSGLV CALDVADQSL
     RMGIIERKLD QLAKRLGVAQ KPQHDVLQFL ADRVPGSIRE LEGAVNTLAA SAGARLGSLT
     LDEAMALLQP NLKVSAERRV TVDEIQKLTA DHFALKQADL LSERRTRSVA RPRQVAMWLC
     KQHTTRSYPD IGRRFGGRDH TTVLHAVKKV EELLQSDEQI AKDVEALTRK LRG
//
DBGET integrated database retrieval system