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Database: UniProt
Entry: D0GPF1_9FUSO
LinkDB: D0GPF1_9FUSO
Original site: D0GPF1_9FUSO 
ID   D0GPF1_9FUSO            Unreviewed;       453 AA.
AC   D0GPF1;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   25-OCT-2017, entry version 52.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:EEY34015.1};
GN   ORFNames=HMPREF0554_0187 {ECO:0000313|EMBL:EEY34015.1};
OS   Leptotrichia goodfellowii F0264.
OC   Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae;
OC   Leptotrichia.
OX   NCBI_TaxID=596323 {ECO:0000313|EMBL:EEY34015.1, ECO:0000313|Proteomes:UP000004226};
RN   [1] {ECO:0000313|EMBL:EEY34015.1, ECO:0000313|Proteomes:UP000004226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0264 {ECO:0000313|EMBL:EEY34015.1,
RC   ECO:0000313|Proteomes:UP000004226};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B.,
RA   Sutton G.G., Strausberg R.L., Nelson K.E.;
RL   Submitted (OCT-2009) 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:SAAS00735475}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00911680}.
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:EEY34015.1}.
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DR   EMBL; ADAD01000192; EEY34015.1; -; Genomic_DNA.
DR   RefSeq; WP_006808371.1; NZ_ADAD01000192.1.
DR   STRING; 596323.HMPREF0554_0187; -.
DR   EnsemblBacteria; EEY34015; EEY34015; HMPREF0554_0187.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000004226; 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   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; 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   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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000004226};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004226}.
FT   DOMAIN      145    284       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      361    430       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     153    160       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   453 AA;  52221 MW;  69CA5827A6DB90EE CRC64;
     MDVNASNLWD KILKIFKNNT SMETEYNAFF KNVKADDFSN NILSLNCNSP LMKEKMEKYK
     NEIEETLNDI FILSNEKIHI VFNIKKEEEP GEISYRIKEY RSTNQNSSMK TGLNVRNRLD
     NFIVGDNSRM AYNACLAVLE NEAPVYNPLF IYGGSGLGKT HLMQAVGNAI LERNPEKRVL
     YTTTEEFSNE FIAAIKEGRI KNFRDTFRNL DVLLLDDIQF FERIFGRGMG DTEEEFFHTF
     NKLQESGKQI IMISDRYPQD IKNLSKRLES RFISGLSTEI LEPGYETRKA ILENIVEIKN
     IEIDDNILEY IAESVSSNVR ELEGILTLIN ARAKLLNEKI TLQQVQDELS TRMRSQQSKI
     TAEKIIEIVS QEYSIPVSEM KARKKKQEIV DARQTAMFLI KNILDLNLTT IGGLFGGKDH
     STVISSIRKI EGKIEENIAF KKELDRIKQK IVK
//
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