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Database: UniProt
Entry: E0UGG0_CYAP2
LinkDB: E0UGG0_CYAP2
Original site: E0UGG0_CYAP2 
ID   E0UGG0_CYAP2            Unreviewed;       454 AA.
AC   E0UGG0;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-SEP-2017, entry version 55.
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=Cyan7822_0001 {ECO:0000313|EMBL:ADN12055.1};
OS   Cyanothece sp. (strain PCC 7822).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Cyanothecaceae; Cyanothece.
OX   NCBI_TaxID=497965 {ECO:0000313|EMBL:ADN12055.1, ECO:0000313|Proteomes:UP000008206};
RN   [1] {ECO:0000313|Proteomes:UP000008206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7822 {ECO:0000313|Proteomes:UP000008206};
RX   PubMed=21972240; DOI=10.1128/mBio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M.,
RA   Min H., Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a
RT   group of unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(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; CP002198; ADN12055.1; -; Genomic_DNA.
DR   RefSeq; WP_013320165.1; NC_014501.1.
DR   STRING; 497965.Cyan7822_0001; -.
DR   EnsemblBacteria; ADN12055; ADN12055; Cyan7822_0001.
DR   KEGG; cyj:Cyan7822_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000008206; 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; 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:UP000008206};
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:UP000008206}.
FT   DOMAIN      145    278       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      354    423       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     153    160       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   454 AA;  51621 MW;  B1F3164F91BAAA05 CRC64;
     MELSPQDLWT QVLERLQSRL SRPAFETWIT TAKVEQLTEK YLVICAANPF ILNHLQKNYL
     QIIADVVEEI LGYPIDIQLT AAQGENIAII GETEMSAYHP STSLGDNPKP IKLNPKYTFS
     RFVVGPNNRL AHAATLAVAE SPGREFNPLF LCGGVGLGKT HLMQAIAHYR LEMYPDSKVF
     YVSTEQFTND LIAAIRQDSL QSFREHYRTA DILLVDDIQF IEGKEYTQEE FFHTFNTLHE
     AGKQVVIASD RPPKQIPTLQ DRLISRFSMG LIADIQVPDL ETRMAILQKK AEYENMRLPR
     EVIEYIATHY TSNIRELEGA LIRAITYIAI SGLSMTVENL APVLNPPLER GEVSPEVILN
     IIAETFHVSV EDLKSNSRRR EISLARQIGM YLMRQHTELS LPRIGEEFGG KDHTTVMYSY
     DKINQLQKKD LELSQTLSQL SDRILLASRT QKTT
//
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