GenomeNet

Database: UniProt
Entry: A0A0G0HI02_9BACT
LinkDB: A0A0G0HI02_9BACT
Original site: A0A0G0HI02_9BACT 
ID   A0A0G0HI02_9BACT        Unreviewed;       487 AA.
AC   A0A0G0HI02;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   20-DEC-2017, entry version 21.
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   ORFNames=US24_C0019G0009 {ECO:0000313|EMBL:KKQ11684.1};
OS   candidate division WS6 bacterium GW2011_GWC2_36_7.
OC   Bacteria; Candidatus Dojkabacteria.
OX   NCBI_TaxID=1619091 {ECO:0000313|EMBL:KKQ11684.1, ECO:0000313|Proteomes:UP000034075};
RN   [1] {ECO:0000313|EMBL:KKQ11684.1, ECO:0000313|Proteomes:UP000034075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a
RT   large radiation of phyla.";
RL   Nature 0:0-0(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, ECO:0000256|SAAS:SAAS00747914}.
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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KKQ11684.1}.
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; LBSF01000019; KKQ11684.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKQ11684; KKQ11684; US24_C0019G0009.
DR   PATRIC; fig|1619091.4.peg.259; -.
DR   Proteomes; UP000034075; Unassembled WGS sequence.
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; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747950};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000034075};
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:UP000034075}.
FT   DOMAIN      183    317       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      395    464       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     191    198       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      132    152       {ECO:0000256|SAM:Coils}.
FT   COILED      347    367       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   487 AA;  56090 MW;  AB754631E6C774DE CRC64;
     MDKAEFNTHV QELPKPEISV ASSYIQTLDP DALWRSTKEN LKLMIGAEEF KNTFGGCYIE
     NISNGVAQVS CDVPYKREKM LRDYRLALKD ALLKSCGQNL EIEINLREGE AVKEKPKYEY
     HDPRTNQTVD LFSAAENEKS LKEENLKKAQ LNPRYLFSNF IVGTNNRLAE AIAQAVVDSL
     GEAYNPVFFH GNTGVGKTHL MQAIGNEVIN RFPEKKVVYI SIEQFLNEMV DSIRTKRNED
     FRNKYRAVDL LIIDDVQFVE TYPRTQEELF HTFNTLYQAN KQIVLASDRP PKEIKNITDR
     LRSRFEGGMV ADIQAPDYET RLAILQQMII DKGSNVNVPK EYLDLIAKNV ENNIRELEGA
     LTKVLSLFKL GMNPTYEDIG RLLQIDLESK RKKISPAKVM KCVSESFDVK LADIKGDRRT
     AYIAQCRQIV MYILRNELGM PLERVAKEVN RKDHTTVLHA CEKIKALREK DSRFNEKMQN
     CYKLIRE
//
DBGET integrated database retrieval system