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Database: UniProt
Entry: A0ZAK2_NODSP
LinkDB: A0ZAK2_NODSP
Original site: A0ZAK2_NODSP 
ID   A0ZAK2_NODSP            Unreviewed;       459 AA.
AC   A0ZAK2;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   05-JUL-2017, entry version 68.
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   ORFNames=NSP_10 {ECO:0000313|EMBL:AHJ26358.1};
OS   Nodularia spumigena CCY9414.
OC   Bacteria; Cyanobacteria; Nostocales; Aphanizomenonaceae; Nodularia.
OX   NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ26358.1, ECO:0000313|Proteomes:UP000019325};
RN   [1] {ECO:0000313|EMBL:AHJ26358.1, ECO:0000313|Proteomes:UP000019325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ26358.1};
RX   PubMed=23555932;
RA   Voss B., Bolhuis H., Fewer D.P., Kopf M., Moke F., Haas F.,
RA   El-Shehawy R., Hayes P., Bergman B., Sivonen K., Dittmann E.,
RA   Scanlan D.J., Hagemann M., Stal L.J., Hess W.R.;
RT   "Insights into the physiology and ecology of the brackish-water-
RT   adapted Cyanobacterium Nodularia spumigena CCY9414 based on a genome-
RT   transcriptome analysis.";
RL   PLoS ONE 8:E60224-E60224(2013).
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; CP007203; AHJ26358.1; -; Genomic_DNA.
DR   RefSeq; WP_006194444.1; NZ_CP007203.1.
DR   ProteinModelPortal; A0ZAK2; -.
DR   STRING; 313624.N9414_05205; -.
DR   EnsemblBacteria; AHJ26358; AHJ26358; NSP_10.
DR   PATRIC; fig|313624.11.peg.1; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   Proteomes; UP000019325; 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:UP000019325};
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:UP000019325}.
FT   DOMAIN      151    279       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      360    429       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     159    166       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   459 AA;  52496 MW;  C54C911A8F9DA5A4 CRC64;
     MEIPIDNLWS QVLERLQLEL SRPTFETWIK TAHAERLENN CLVIITPNPF ARNWLQKYYI
     NTIANVVQDI LGHTVEIYLT VAQGDEMTNL GESEVTWELP SQSMTAESVP QNKQPPKDLN
     SKYVFSRFVV GANNRMAHAA SLAVAESPGR EFNPLFLCGG VGLGKTHLMQ AIGHYRSQIC
     PDSKIFYVST EQFTNDLITA IRNDSMQNFR EHYRAADVLL VDDIQFIEGK EYTQEEFFHT
     FNTLHEAGKQ VVIASDRPPH HIPQLQERLC SRFSMGLIAD VQTPDLETRM AILQKKAEYE
     NIRLPRDVIE YIASNYTNNI RELEGALIRA LAYISIWGLP MTVENITPVL ERQSEKVAAT
     PEVILSVIGD NFAISIEDLK SNSRRREISW ARQIGMYLMR QHTDLSLPRI GEEFGGKDHT
     TVIYSCDKIA QLLQSDRTLV QTLRQLSDRI NMNSKQQRQ
//
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