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Database: UniProt
Entry: D7DJN0_METV0
LinkDB: D7DJN0_METV0
Original site: D7DJN0_METV0 
ID   D7DJN0_METV0            Unreviewed;       471 AA.
AC   D7DJN0;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   30-AUG-2017, entry version 51.
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   OrderedLocusNames=M301_0001 {ECO:0000313|EMBL:ADI28390.1};
OS   Methylotenera versatilis (strain 301).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylotenera.
OX   NCBI_TaxID=666681 {ECO:0000313|EMBL:ADI28390.1, ECO:0000313|Proteomes:UP000000383};
RN   [1] {ECO:0000313|Proteomes:UP000000383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 {ECO:0000313|Proteomes:UP000000383};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Clum A., Land M., Hauser L., Kyrpides N., Ivanova N.,
RA   Chistoservova L., Kalyuzhnaya M., Woyke T.;
RT   "Complete sequence of Methylotenera sp. 301.";
RL   Submitted (MAY-2010) 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}.
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DR   EMBL; CP002056; ADI28390.1; -; Genomic_DNA.
DR   RefSeq; WP_013146708.1; NC_014207.1.
DR   STRING; 666681.M301_0001; -.
DR   EnsemblBacteria; ADI28390; ADI28390; M301_0001.
DR   KEGG; meh:M301_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000000383; Chromosome.
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:UP000000383};
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:UP000000383}.
FT   DOMAIN      168    298       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      379    448       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     176    183       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   471 AA;  53840 MW;  718044EE42A533FB CRC64;
     MENFWPTCLS RFEQELSTQQ FNTWIKPLHA EVEGNAVRLV APNRFVMQWV KERFLKKIEQ
     FAHDLHLANI KIDFVISDSD QKNSAEKPAA KQTSKVEIST NINLMESKIS QISQAISTSK
     NINKKTSESS KVSSGLNSAF NFDNYVTGRA NQLARAAAIQ VAENPGTAYN PLFIYGGVGL
     GKTHLLQAIG NELKKHNPDA KIRYLHAERY VTDVVKAYEH KAFDEFKRQY HSLDLLLIDD
     IQFFAKKTRT QEEFFYAFNS LIEAKKQIVI TCDTYPKEII DVDERLRTRF SWGLTVAVEP
     PELEMRVAIL LKKAEAVNLN LPEDVAFFIA KQIRSSVREL EGALNRIIAM AKFTGHSIDV
     HLAKDALRDL IAVRGRQVTM ENIQKTVADY YKIKVAEMYS KKRTRNFARP RQIAMALSRE
     LTNHSFPEIG EAFGGRHHTT VMHACDEVDL LRQNDPTFTR DISFLVQVIR D
//
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