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Database: UniProt
Entry: A0A0C2QGW7_9CYAN
LinkDB: A0A0C2QGW7_9CYAN
Original site: A0A0C2QGW7_9CYAN 
ID   A0A0C2QGW7_9CYAN        Unreviewed;       462 AA.
AC   A0A0C2QGW7;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   05-JUL-2017, entry version 22.
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=SD81_12595 {ECO:0000313|EMBL:KIJ77520.1};
OS   Tolypothrix campylonemoides VB511288.
OC   Bacteria; Cyanobacteria; Nostocales; Tolypothrichaceae; Tolypothrix.
OX   NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ77520.1, ECO:0000313|Proteomes:UP000031981};
RN   [1] {ECO:0000313|EMBL:KIJ77520.1, ECO:0000313|Proteomes:UP000031981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VB511288 {ECO:0000313|EMBL:KIJ77520.1,
RC   ECO:0000313|Proteomes:UP000031981};
RA   Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT   "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT   VB511288.";
RL   Submitted (JAN-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: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:KIJ77520.1}.
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DR   EMBL; JXCB01000007; KIJ77520.1; -; Genomic_DNA.
DR   RefSeq; WP_041035168.1; NZ_JXCB01000007.1.
DR   EnsemblBacteria; KIJ77520; KIJ77520; SD81_12595.
DR   Proteomes; UP000031981; 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:UP000031981};
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:UP000031981}.
FT   DOMAIN      153    281       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      362    431       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     161    168       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   462 AA;  52760 MW;  886E28A1972DE3A7 CRC64;
     MEIAIENLWS QVLERLQLEL SRPTFETWIK TASAQRLENN CLVICTPNPF ARNWLQKYYI
     KTIAHVVQDI LGYPVDIYIT VTNDESTNDE SPVSEEVSSG FPDQTSIAET LPQNRLNTPE
     LNPKYVFSRF VVGANNRMAH AASLAVAEYP GREFNPLFLC GGVGLGKTHL MQAIGHYRLE
     ICPDSRIFYV STEQFTNDLI TAIRKDSMQS FREHYRAADV LLVDDIQFIE GKEYTQEEFF
     HTFNTLHEAG KQVVLASDRP PNQIPQLQER LCSRFSMGLI ADIQAPDLET RMAILQKKAE
     YENIRLPRDV VEYIASHYTS NIRELEGALI RALAYISIWG LPMTVENLAP ILEPPTQKGE
     ATPEGILTVI AEVFDVPIED LKGNSRRREI SWARQIAMYL MRRHTDLSLP RIGEEFGGKD
     HTTVMYSCEK IAQLQQTDQN LVQTLRQLSD RINMASRPKK SY
//
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