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Database: UniProt
Entry: G0G4F5_AMYMS
LinkDB: G0G4F5_AMYMS
Original site: G0G4F5_AMYMS 
ID   G0G4F5_AMYMS            Unreviewed;       547 AA.
AC   G0G4F5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   25-OCT-2017, entry version 50.
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   ECO:0000313|EMBL:AEK38496.1};
GN   OrderedLocusNames=RAM_00005 {ECO:0000313|EMBL:AEK38496.1};
OS   Amycolatopsis mediterranei (strain S699) (Nocardia mediterranei).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=713604 {ECO:0000313|EMBL:AEK38496.1, ECO:0000313|Proteomes:UP000006138};
RN   [1] {ECO:0000313|EMBL:AEK38496.1, ECO:0000313|Proteomes:UP000006138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S699 {ECO:0000313|EMBL:AEK38496.1,
RC   ECO:0000313|Proteomes:UP000006138};
RX   PubMed=21914879; DOI=10.1128/JB.05819-11;
RA   Verma M., Kaur J., Kumar M., Kumari K., Saxena A., Anand S., Nigam A.,
RA   Ravi V., Raghuvanshi S., Khurana P., Tyagi A.K., Khurana J.P., Lal R.;
RT   "Whole genome sequence of the rifamycin B-producing strain
RT   Amycolatopsis mediterranei S699.";
RL   J. Bacteriol. 193:5562-5563(2011).
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}.
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DR   EMBL; CP002896; AEK38496.1; -; Genomic_DNA.
DR   RefSeq; WP_013221955.1; NC_018266.1.
DR   EnsemblBacteria; AEK38496; AEK38496; RAM_00005.
DR   KEGG; amm:AMES_0001; -.
DR   KEGG; amn:RAM_00005; -.
DR   PATRIC; fig|713604.12.peg.1; -.
DR   KO; K02313; -.
DR   OMA; ATHIERN; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000006138; Chromosome.
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:UP000006138};
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:UP000006138}.
FT   DOMAIN      239    367       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      451    520       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     247    254       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   547 AA;  60671 MW;  46DE8E6E8D1E953F CRC64;
     MSDHQHNLGV IWEQVVRELS DGTLSPQQRA WMRVTRPIGL LDGTALLAAP SDFAKEAIER
     GLRGAITDAL SRRLGRAISL AVKVDSAEAV APAPAPHYAP SPGRVENGTS PEPAPPMPAN
     GAPMMPPPRP AEPAQQRPPM PRPPMSMPAH QSVAPKPDDG DDTDEEVDEE GEALAAVHEI
     WPTFSGQPIA GQPYTAPAQP QTSKTKLNEK YTFDTFVIGA SNRFAHAAAV AVAEAPARAY
     NPLFIWGESG LGKTHLLHAV GHYAQRLFPG MRVRYVSTEE FTNDFINSLR DDRKVAFQRR
     YRDIDILLVD DIQFLEGKEG TQEEFFHTFN TLHNANKQIV VSSDRPPKRL ETLEDRLRTR
     FEWGLITDIQ PPELETRIAI LRKKAAQDRL AVPGEVLEFI ASRVEANIRE LEGALIRVTA
     FASLNQQPVD SALAEIVLRD LIPDSHAPEI TAPTIMGVTS EFFDVTLDDL CGPGKTKALA
     TARQIAMYLC RELTDMSLPK IGQTFGGRDH TTVMHADKKI RKEMAERRRI YDQVQELTSR
     IKQRARQ
//
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