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Database: UniProt
Entry: A0A164D074_9SYNE
LinkDB: A0A164D074_9SYNE
Original site: A0A164D074_9SYNE 
ID   A0A164D074_9SYNE        Unreviewed;       475 AA.
AC   A0A164D074;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   05-JUL-2017, entry version 10.
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   ECO:0000313|EMBL:KZR91031.1};
GN   ORFNames=MITS9508_00268 {ECO:0000313|EMBL:KZR91031.1};
OS   Synechococcus sp. MIT S9508.
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1801629 {ECO:0000313|EMBL:KZR91031.1, ECO:0000313|Proteomes:UP000076799};
RN   [1] {ECO:0000313|EMBL:KZR91031.1, ECO:0000313|Proteomes:UP000076799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT S9508 {ECO:0000313|EMBL:KZR91031.1,
RC   ECO:0000313|Proteomes:UP000076799};
RA   Cubillos-Ruiz A., Berta-Thompson J.W., Becker J.W., Chisholm S.W.;
RT   "Evolutionary Radiation of Lanthipeptides in Marine
RT   Picocyanobacteria.";
RL   Submitted (FEB-2016) 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: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}.
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:KZR91031.1}.
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DR   EMBL; LVHU01000001; KZR91031.1; -; Genomic_DNA.
DR   EnsemblBacteria; KZR91031; KZR91031; MITS9508_00268.
DR   PATRIC; fig|1801629.3.peg.292; -.
DR   Proteomes; UP000076799; Unassembled WGS sequence.
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:UP000076799};
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:UP000076799}.
FT   DOMAIN      168    291       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      377    446       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     176    183       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   475 AA;  52299 MW;  0DAB5D8B69BD6DCF CRC64;
     MRRFSHRDSE GVVLTGSELW SKVQQALQSN LSKPTFETWI RPAQCGGFRE GTLTLLAPNS
     FARNWLRKNY ASAIADVAGE IIGQPVTVSV LARDAEDLQA GSAPAAVTAA ASAAAVPAPL
     APPTPAKKAP RRLPGLNMRY VFNRFVVGPN SRMAHAAALA VAEAPGREFN PLFICGGVGL
     GKTHLMQAIG HYRLEIDPEA KVFYVSTETF TNDLIVAIRK DGMQAFRDRY RAADLILVDD
     IQFIEGKEYT QEEFFHTFNA LHEAGRQIVI ASDRPPSQIP RLQERLISRF SMGLIADIQA
     PDLETRMAIL QKKAEQERVA LPRDLIQYIS GRFTSNIREL EGALTRAVAF SSITGMPMTV
     ESVAPMLNPS GQGVDVTPQQ VIDKVSEVFG VTADDMRSSS RRRAVSQARQ VGMFLMRQGT
     GLSLPRIGET FGGKDHTTVM YAIEQVEKKL GNDPQLASQV QRVRDLLQID SRRKR
//
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