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Database: UniProt
Entry: W5VX16_9PSEU
LinkDB: W5VX16_9PSEU
Original site: W5VX16_9PSEU 
ID   W5VX16_9PSEU            Unreviewed;       517 AA.
AC   W5VX16;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   25-OCT-2017, entry version 30.
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=KALB_1 {ECO:0000313|EMBL:AHH93378.1};
OS   Kutzneria albida DSM 43870.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Kutzneria.
OX   NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH93378.1, ECO:0000313|Proteomes:UP000019225};
RN   [1] {ECO:0000313|EMBL:AHH93378.1, ECO:0000313|Proteomes:UP000019225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH93378.1};
RX   PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA   Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA   Bechthold A., Kalinowski J., Luzhetskyy A.;
RT   "Complete genome sequence of producer of the glycopeptide antibiotic
RT   Aculeximycin Kutzneria albida DSM 43870T, a representative of minor
RT   genus of Pseudonocardiaceae.";
RL   BMC Genomics 15:885-885(2014).
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; CP007155; AHH93378.1; -; Genomic_DNA.
DR   RefSeq; WP_025353671.1; NZ_CP007155.1.
DR   EnsemblBacteria; AHH93378; AHH93378; KALB_1.
DR   KEGG; kal:KALB_1; -.
DR   PATRIC; fig|1449976.3.peg.1; -.
DR   KO; K02313; -.
DR   Proteomes; UP000019225; 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:UP000019225};
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:UP000019225}.
FT   DOMAIN      209    337       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      421    490       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     217    224       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   517 AA;  57533 MW;  D3DA0D68DDDD5A61 CRC64;
     MSDDQTNLGQ VWDQVVQELL AAGALSSLQR AWMRVTRPIG LLDGTVLLGA PSDFAKEAIE
     RALRDPITAA LSRRLNRPVS LAVKVDTVVP PAASTPPPVP QPPPLNGSPR PPAVAPMEQT
     APMPAIPAED SSAAEDDDAT EVDEEREALA TVHEIWPTFS GNPAVQPSSQ TNSQTRLNEK
     YTFETFVIGA SNRFAHAAAV AVAEAPARAY NPLFIWGESG LGKTHLLHAV GHYAQRLFPG
     MRVRYVSTEE FTNDFINSLR DDRKVAFQRR YRDIDVLLVD DIQFLEGKEG TQEEFFHTFN
     TLHNANKQIV VSSDRPPKRL ETLEDRLRTR FEWGLITDIQ PPELETRIAI LRKKAAQDRL
     AAPAEVLEFI AARIERNIRE LEGALIRVTA FASLNRQPVD VQLAEIVLRD LIPDSHAPEI
     TAPTIMAVTA EFFGVSIDDL CGPGKTKALA QARQISMYLC RELTDLSLPK IGQTFGGRDH
     TTVMHADKKI RKEMAERRRI YDQVQELTSR IKQRARS
//
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