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Database: UniProt
Entry: A0A120MG75_9BRAD
LinkDB: A0A120MG75_9BRAD
Original site: A0A120MG75_9BRAD 
ID   A0A120MG75_9BRAD        Unreviewed;       477 AA.
AC   A0A120MG75;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   25-OCT-2017, entry version 15.
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_1 {ECO:0000313|EMBL:AMH39606.1};
GN   Synonyms=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=A4A58_03915 {ECO:0000313|EMBL:KZD25563.1}, PROKKA_00795
GN   {ECO:0000313|EMBL:AMH39606.1};
OS   Tardiphaga robiniae.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Tardiphaga.
OX   NCBI_TaxID=943830 {ECO:0000313|EMBL:AMH39606.1};
RN   [1] {ECO:0000313|EMBL:AMH39606.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Vaf07 {ECO:0000313|EMBL:AMH39606.1};
RA   Kopat V.;
RT   "Evolution marks in rhizobial microsymbionts genomes from the relict
RT   species Vavilovia formosa (Stev.) Fed.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KZD25563.1, ECO:0000313|Proteomes:UP000076574}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vaf07 {ECO:0000313|EMBL:KZD25563.1,
RC   ECO:0000313|Proteomes:UP000076574};
RA   Kopat V., Chirak E., Kimeklis A., Andronov E.;
RT   "Microsymbionts genomes from the relict species Vavilovia formosa
RT   (Stev.) Fed.";
RL   Submitted (MAR-2016) 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: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; KT955714; AMH39606.1; -; Genomic_DNA.
DR   EMBL; LVYV01000001; KZD25563.1; -; Genomic_DNA.
DR   RefSeq; WP_068729936.1; NZ_LVYV01000001.1.
DR   EnsemblBacteria; KZD25563; KZD25563; A4A58_03915.
DR   Proteomes; UP000076574; 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; 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:UP000076574};
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:UP000076574}.
FT   DOMAIN      170    296       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      385    454       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     178    185       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   477 AA;  53010 MW;  897421C4E2683443 CRC64;
     MANMEQDHWS RVKGRLRSTV GEDVYSSWFA RMDLESVQDD SVHLSVPTRF LKSWIQAHYA
     ERVLNAWQAE MPQVHRVDLT VRSAMRNVAP ANKEAAAPAE ARRTETSNNR HAPELRATAT
     APVSASHEAL GGSPLDPRLT FASFVLGRAN TLAHAAARQV AEGRRGDPVM FNPLYIHAGV
     GLGKTHLLQA VTWAGNSGPD RKVLYLTAEK FMYGFVAALK TQTALAFKEA LRGIDVLVID
     DMQFLQGKTT QAEFCHTLNA LIDAGRQVVI AADRPPSDLE SLDERVRSRL AGGLVVEMSS
     LGEELRLGIL KSRVAAARAH HASFEVPEPV LDYLARTITH NGRDLEGAIN RLLAHSKLNA
     TPVTLEMAER EVRDLIRPQE PKRIKIEDIQ RVVARQYNVS RSDLLSSRRT ANVVRPRQVA
     MYLAKTLTLR SLPEIGRRFG GRDHTTVLHA VRKIEALVGK DVALQDEVET LKRQLQE
//
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