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Database: UniProt
Entry: D1ADA0_THECD
LinkDB: D1ADA0_THECD
Original site: D1ADA0_THECD 
ID   D1ADA0_THECD            Unreviewed;       721 AA.
AC   D1ADA0;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   05-JUL-2017, entry version 64.
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 {ECO:0000256|HAMAP-Rule:MF_00377};
GN   OrderedLocusNames=Tcur_0001 {ECO:0000313|EMBL:ACY95610.1};
OS   Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 /
OS   NBRC 15933 / NCIMB 10081 / Henssen B9).
OC   Bacteria; Actinobacteria; Streptosporangiales; Thermomonosporaceae;
OC   Thermomonospora.
OX   NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY95610.1, ECO:0000313|Proteomes:UP000001918};
RN   [1] {ECO:0000313|EMBL:ACY95610.1, ECO:0000313|Proteomes:UP000001918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 /
RC   Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX   PubMed=21475583; DOI=10.4056/sigs.1453580;
RA   Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S.,
RA   Del Rio T.G., Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A.,
RA   Chen A., Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Han C., Detter J.C., Rohde M., Goker M.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Thermomonospora curvata type strain
RT   (B9).";
RL   Stand. Genomic Sci. 1:13-22(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:SAAS00724167}.
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; CP001738; ACY95610.1; -; Genomic_DNA.
DR   RefSeq; WP_012850394.1; NC_013510.1.
DR   ProteinModelPortal; D1ADA0; -.
DR   STRING; 471852.Tcur_0001; -.
DR   EnsemblBacteria; ACY95610; ACY95610; Tcur_0001.
DR   KEGG; tcu:Tcur_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000001918; Chromosome.
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; IPR024633; DnaA_N_dom.
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   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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001918};
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:UP000001918}.
FT   DOMAIN      412    540       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      624    693       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     420    427       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   721 AA;  78681 MW;  A5A28ABDE85F46E3 CRC64;
     MEGRDLTAVW ARTLAALSEG DLPPSYRAWL PLVRPLALVE GTALLAAPNE FAKDALETRL
     RGLITQALSA ELGREIRVAV TVQPEPPSDP APADRAQPAP PAYRGQSHPG VIHSPGGAGG
     YPEGGYGGPV GQGYPPPRDG GHDDSDHDGV HPPGRHRAYQ PHPGDYEGRH AGGHDRDGEP
     GHHRGPEAAP HGEESPWRPG VHMPPHLSDR PGGALHYENR YEEGAGRAGE NSADLGTHHD
     HQGAAPRPDD PHRPFADRPF GEGAGRPGEG PGLFPIPDAR HSAEGMLPAD PAPPGQGRHR
     SDEHGHGEAG HLPPPGQGPR PYEGTFTGPF GQPPADGPLN QGRPAGGRAD RPGDGGEHEQ
     QPWQRRPAAE PRPGSEHARL NPKYTFETFV IGSSNRFAHA AAVAVAEQPA KAYNPLFIYG
     DSGLGKTHLL HAIGHYAQSL FSGVRVRYVS SEEFTNDFIN AIRDGKADHF RRRYRDIDIL
     LVDDIQFLEG KEQTQEEFFH TFNTLHNASK QIVISSDRPP KDLVTLEDRL RNRFEWGLTT
     DVQPPELETR IAILQKKARQ EGLAVPQDVV EFIASQIATN IRELEGALIR VTAYASLNRQ
     SVDMRVAETV LKDLIPDDSG PEITAAMIMA QTVEYFGTTI EDLCGPSRSR MLVTARQIAM
     YLCRELTDLS LPKIGAQFGG RDHTTVMHAE RKIRALMAER RAIYNQVTEL TGRIKNQARK
     R
//
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