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Database: UniProt
Entry: A0A0M1JRH0_9CYAN
LinkDB: A0A0M1JRH0_9CYAN
Original site: A0A0M1JRH0_9CYAN 
ID   A0A0M1JRH0_9CYAN        Unreviewed;       468 AA.
AC   A0A0M1JRH0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   16-JAN-2019, entry version 24.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=AM228_15865 {ECO:0000313|EMBL:KOR35826.1};
OS   Planktothricoides sp. SR001.
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Planktothricoides.
OX   NCBI_TaxID=1705388 {ECO:0000313|EMBL:KOR35826.1, ECO:0000313|Proteomes:UP000037054};
RN   [1] {ECO:0000313|Proteomes:UP000037054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SR001 {ECO:0000313|Proteomes:UP000037054};
RA   Tan B., Te S.H., Thompson J., Gin K.;
RT   "Draft Genome of Planktothricoides sp. SR001.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC       ECO:0000256|SAAS:SAAS00555179}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KOR35826.1}.
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DR   EMBL; LIUQ01000026; KOR35826.1; -; Genomic_DNA.
DR   RefSeq; WP_054467085.1; NZ_LIUQ01000026.1.
DR   EnsemblBacteria; KOR35826; KOR35826; AM228_15865.
DR   PATRIC; fig|1705388.3.peg.5261; -.
DR   OrthoDB; 219876at2; -.
DR   Proteomes; UP000037054; Unassembled WGS sequence.
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   Gene3D; 3.30.300.180; -; 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; IPR038454; DnaA_N_sf.
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   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:SAAS00756129};
KW   Complete proteome {ECO:0000313|Proteomes:UP000037054};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037054}.
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   468 AA;  53377 MW;  9850D71A0ACA0CD6 CRC64;
     MATPLEHLWN QVLERLQLQL SRPTFETWIK TAKAEQLENY CLVIRTPNPF ARNWLQKYYV
     KTIAEVVQEI LQHPVEIYIT TDQAEIVCGT EAAEYIWPSP TPGGGIETSL GPRPRPSELN
     LKYNFSSFVV GSNNRMAHAA SLAVAESPGR EFNPLFLCGG VGLGKTHLMQ AIGHYRLEIA
     PNTRIFYVST EQFTNDLIVA IRKDSMQSFR EHYRAADVLL VDDIQFIEGK EYTQEEFFHT
     FNTLHEAGKQ VVLAADRPPN QIPRLQERLC SRFSMGLIAD IQPPDLETRM AILQKKAEYE
     NMRLPRDVIE YIARQFTSNI RELEGALIRT VAYISISGLP MTVQNIAPIL NPQTEKLEAT
     PEAVMNAVIS IFGVSMEELK GNSRRREISQ ARQIAMYLMR QHTDLSLPKI GEEFGGKDHT
     TVLYSCEKIA QRIQQDPDLA NILRQLNDRI HLANRQGSES APHRYRDR
//
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