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Database: UniProt
Entry: A0A0G0J1X2_9BACT
LinkDB: A0A0G0J1X2_9BACT
Original site: A0A0G0J1X2_9BACT 
ID   A0A0G0J1X2_9BACT        Unreviewed;       480 AA.
AC   A0A0G0J1X2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   25-OCT-2017, entry version 18.
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=US82_C0026G0011 {ECO:0000313|EMBL:KKQ60952.1};
OS   Parcubacteria group bacterium GW2011_GWC1_38_22.
OC   Bacteria; unclassified Parcubacteria group.
OX   NCBI_TaxID=1618897 {ECO:0000313|EMBL:KKQ60952.1, ECO:0000313|Proteomes:UP000034773};
RN   [1] {ECO:0000313|EMBL:KKQ60952.1, ECO:0000313|Proteomes:UP000034773}
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}.
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:KKQ60952.1}.
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DR   EMBL; LBUL01000026; KKQ60952.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKQ60952; KKQ60952; US82_C0026G0011.
DR   PATRIC; fig|1618897.3.peg.739; -.
DR   Proteomes; UP000034773; 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; 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.
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:UP000034773};
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:UP000034773}.
FT   DOMAIN      175    307       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      387    456       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     183    190       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   480 AA;  54421 MW;  FA59494429ABD1C3 CRC64;
     MNNAELWQAA LGEIELSISK ANFSTWFKNT TILSNENGKV VIGVPNGFAK EWLENKYNTY
     IFRALRNFQD DIREISCVIY SSDPAPQNGQ GEMKKNEPMS AQSQQPPQAY QQPQQAVQQA
     GNYAPRPIQN TNHAGLTAQE NNINPRYTFE NFIIGENNEL ARAACYAVSQ NLGKIYNPLF
     IYGGVGLGKT HLLQSIGNEV LAHDSSRRIK YITSERFANE LIDSIRNQTV NDFKSAYQAI
     DLLIIDDVQF LAGKEKTQIE FFHIFNALYQ LNKQIVISSD RPPKAIATLE DRLRSRFEGG
     MIADIGKPDL ETRIAILKTK TAERNFYMDE EALRFIAENV KNNIRELEGA LNRIIGACEF
     NKKLPTLKFV QQALQEIISS GKKKGVQPQN VIDAIAQYFN ISNKELIEKG RKKEIAYARH
     IAMYIMRSEL SSSYPSIGTI FGGRDHTTAL HAFEKISKEM ETDEKVREDV SILRERIYAV
//
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