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Database: UniProt
Entry: A0A0D0X4G1_9ACTN
LinkDB: A0A0D0X4G1_9ACTN
Original site: A0A0D0X4G1_9ACTN 
ID   A0A0D0X4G1_9ACTN        Unreviewed;       631 AA.
AC   A0A0D0X4G1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   25-OCT-2017, entry version 24.
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=TK50_01575 {ECO:0000313|EMBL:KIR64405.1};
OS   Micromonospora carbonacea.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Micromonospora.
OX   NCBI_TaxID=47853 {ECO:0000313|EMBL:KIR64405.1, ECO:0000313|Proteomes:UP000032254};
RN   [1] {ECO:0000313|EMBL:KIR64405.1, ECO:0000313|Proteomes:UP000032254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JXNU-1 {ECO:0000313|EMBL:KIR64405.1,
RC   ECO:0000313|Proteomes:UP000032254};
RA   Long Z., Huang Y., Jiang Y.;
RT   "Sequencing and annotation of Micromonospora carbonacea strain JXNU-1
RT   genome.";
RL   Submitted (JAN-2015) 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   -!- 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:KIR64405.1}.
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DR   EMBL; JXSX01000001; KIR64405.1; -; Genomic_DNA.
DR   RefSeq; WP_043961005.1; NZ_JXSX01000001.1.
DR   EnsemblBacteria; KIR64405; KIR64405; TK50_01575.
DR   PATRIC; fig|47853.6.peg.344; -.
DR   Proteomes; UP000032254; 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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000032254};
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:UP000032254}.
FT   DOMAIN      325    453       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      537    606       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     333    340       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      606    631       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   631 AA;  68716 MW;  002D33676D022A9C CRC64;
     MAGTTDLAAV WTATTDELAD EIISAQQRAY LRLTRLRAIV EDTALLSVPD AFTRDVIESR
     LRPAITEALT RRLGRPIQVA VTVRVAEDPS GRPAGTVYRS TPDAGPGEQP ALDGSAGFDS
     AAAFDARGYD ESGAGRHEPA LGFPAPGHPG HDEPGADPAR PPHPGQDGTA GHPGHGAAEP
     GPASRPAPTD DGHRPGLVPA ARDAQEPLFG DAFAEPLVPG ADRRGFEERP RLDVGGARPY
     EGRYAAGAVP APQRLPRDGG TDSGPGRSGM DHRPGGRDDR RLPGGAETGG NRLNPKYMFE
     TFVIGSSNRF AHAASVAVAE SPAKAYNPLF IYGSSGLGKT HLLHAIGHYA TTLGNARSVR
     YVSTEEFTND FINSVRDDKT SAFQRRYRDV DILLIDDIQF LENRERTQEE FFHTFNTLHN
     ANKQIVVTSD RSPKQLATLE DRLRTRFEWG LLADIQPPDL ETRIAILQKK AAQERLYAPP
     DVLEFIASRV SNSIRELEGA LIRVTAFASL TRSTVELSLA EEVLRDFIPD GAGPEITADQ
     IMVSTADYFG VSLEDLRGHS RSRVLVNARQ VAMYLCRELT DLSLPRIGQA FGGRDHTTVM
     HADRKIRQQM AERRSLYNQI AELTNRIKQT T
//
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