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Database: UniProt
Entry: D7B601_NOCDD
LinkDB: D7B601_NOCDD
Original site: D7B601_NOCDD 
ID   D7B601_NOCDD            Unreviewed;       652 AA.
AC   D7B601;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   05-JUL-2017, entry version 55.
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   OrderedLocusNames=Ndas_0001 {ECO:0000313|EMBL:ADH65454.1};
OS   Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115
OS   / JCM 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU
OS   509) (Actinomadura dassonvillei).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Nocardiopsis.
OX   NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH65454.1, ECO:0000313|Proteomes:UP000002219};
RN   [1] {ECO:0000313|EMBL:ADH65454.1, ECO:0000313|Proteomes:UP000002219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC   NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC   {ECO:0000313|Proteomes:UP000002219};
RX   PubMed=21304737; DOI=10.4056/sigs.1363462;
RA   Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H.,
RA   Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Pagani I.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Djao O.D., Rohde M., Sikorski J., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Nocardiopsis dassonvillei type strain
RT   (IMRU 509).";
RL   Stand. Genomic Sci. 3:325-336(2010).
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:SAAS00731907}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00756131}.
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; CP002040; ADH65454.1; -; Genomic_DNA.
DR   RefSeq; WP_013151061.1; NC_014210.1.
DR   STRING; 446468.Ndas_0001; -.
DR   EnsemblBacteria; ADH65454; ADH65454; Ndas_0001.
DR   KEGG; nda:Ndas_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; ATHIERN; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000002219; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
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:SF12; PTHR30050:SF12; 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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002219};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002219}.
FT   DOMAIN      344    474       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      556    624       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     352    359       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   652 AA;  71143 MW;  2CD01B3396FAA96B CRC64;
     MADAQVNLAV VWSSVLDGID NDSLPAHQRA WLPQTRPLGL IEDTALIAAP NEFTKKVLET
     RLYPAISKAL SAHLGREIRV AVTVDPTAVP TPPPTPTPPA APGPQGPRSV EGHTAPAFSP
     VVPGTAPGPT RPTAPPAAPA DAQRAVTGSR GQHARPAAEA AEQPAPWPSA PAPAPEQADL
     LGPTPPADHP SPTDEAPHTV RDAPAPWVQQ TFASPQETPT APPLWEQPSA LERPQEPAGW
     RQQSWTEPEW DRPNRWETPR EEAPAPGAEA AEEAAQPAPE AVEAPVEDEA PKAPSSPPGR
     SQEVPPGEHA RLNPKYTFDT FVIGSSNRFA HAASVAAAEA PAKAYNPLFI HGGSGLGKTH
     LLHAIGHYTH RLYEGSRVRY VSSEEFTNEF INSIRDGKAD GFRRRYRDID VLLVDDIQFL
     ENKEQTQEEF FHTFNTLHNS DKQIVISSDR PPKQLTTLED RMRSRFEWGL LTDVQPPELE
     TRIAILRKKA AQEGLAAPPE VLEFIASKIS TNIRELEGAL IRVTAFASLN RQSVDLDLTS
     QVLRDLVPST EVPEVTAGAI MSQTAAYFGL TVEDLCGTSR SRVLVTARQI AMYLCRELTE
     LSLPKIGQQF GRDHTTVMHA ERKVRGLMAE RRSIYNQVHE LTSRIKDQPS LT
//
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