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Database: UniProt
Entry: A0A0E9M9G9_9PROT
LinkDB: A0A0E9M9G9_9PROT
Original site: A0A0E9M9G9_9PROT 
ID   A0A0E9M9G9_9PROT        Unreviewed;       450 AA.
AC   A0A0E9M9G9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   30-AUG-2017, entry version 19.
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_1 {ECO:0000313|EMBL:GAO34103.1};
GN   Synonyms=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=OYT1_02169 {ECO:0000313|EMBL:GAO34103.1};
OS   Ferriphaselus amnicola.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Gallionellaceae; Ferriphaselus.
OX   NCBI_TaxID=1188319 {ECO:0000313|EMBL:GAO34103.1, ECO:0000313|Proteomes:UP000033070};
RN   [1] {ECO:0000313|EMBL:GAO34103.1, ECO:0000313|Proteomes:UP000033070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OYT1 {ECO:0000313|EMBL:GAO34103.1,
RC   ECO:0000313|Proteomes:UP000033070};
RA   Kato S., Ohkuma M.;
RT   "Draft genome sequence of Ferriphaselus amnicola strain OYT1.";
RL   Submitted (FEB-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:GAO34103.1}.
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DR   EMBL; BBTH01000006; GAO34103.1; -; Genomic_DNA.
DR   RefSeq; WP_062627276.1; NZ_BBTH01000006.1.
DR   EnsemblBacteria; GAO34103; GAO34103; OYT1_02169.
DR   Proteomes; UP000033070; 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:UP000033070};
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:UP000033070}.
FT   DOMAIN      147    278       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      358    427       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     155    162       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   450 AA;  50489 MW;  B95834F7E0C04111 CRC64;
     MPDHPVWVSC LDFFQESLPP QQFNSWIKPL TFDIVGSQIV LTAPNSFALK LIQERFLSVI
     SQRAESLLPF VPTIELKVGK KRIPTTQQTT PETSILPTAP CEASSPKSQK EFGKLNPTLC
     FDHFVTGKAN QLAHAAAIQV ADTPGSVYNP LFIYGGVGLG KTHLLQAIGN QIKSNSPKAK
     VCYIHATNYV SDWVKAVQTK RFDEFKQFYN SLDLLLIDDI QFIADKAGTQ QEFFYTLNTL
     TEAHKQVVIT CDTFPKEISG IEPRLTSRFS WGLTVAVDPP NVEMRVAILL QKASQSKMSL
     GEDVAFFIAK HVRSNIRELE GALKRVEAFS RFHRRPISVE VAKDALKDLL ASQNKQVSID
     NIQKTVADFY RIKVADLLSK KRTRNITRPR QMAMLLAREL TPFSLPEIGA AFGDRDHSTV
     LYACRTIELL KRSNSITNAE YNTLSQSLRN
//
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