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Database: UniProt
Entry: F7NFW3_9FIRM
LinkDB: F7NFW3_9FIRM
Original site: F7NFW3_9FIRM 
ID   F7NFW3_9FIRM            Unreviewed;       487 AA.
AC   F7NFW3;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-SEP-2017, entry version 42.
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:EGO65071.1};
GN   ORFNames=ALO_04733 {ECO:0000313|EMBL:EGO65071.1};
OS   Acetonema longum DSM 6540.
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Acetonema.
OX   NCBI_TaxID=1009370 {ECO:0000313|EMBL:EGO65071.1, ECO:0000313|Proteomes:UP000003240};
RN   [1] {ECO:0000313|EMBL:EGO65071.1, ECO:0000313|Proteomes:UP000003240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6540 {ECO:0000313|EMBL:EGO65071.1,
RC   ECO:0000313|Proteomes:UP000003240};
RX   PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA   Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA   Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA   Jensen G.J.;
RT   "Structural diversity of bacterial flagellar motors.";
RL   EMBO J. 30:2972-2981(2011).
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:EGO65071.1}.
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DR   EMBL; AFGF01000037; EGO65071.1; -; Genomic_DNA.
DR   RefSeq; WP_004093301.1; NZ_AFGF01000037.1.
DR   STRING; 1009370.ALO_04733; -.
DR   EnsemblBacteria; EGO65071; EGO65071; ALO_04733.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000003240; 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; 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:UP000003240};
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:UP000003240}.
FT   DOMAIN      182    310       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      394    463       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     190    197       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   487 AA;  55823 MW;  0F53A9AFE30EDC1B CRC64;
     MNDTPNTAEL AQTWEKIIQI LEKEVIKPIF NTWIKSTIPL SITDTTFEIG TPTDFCKEWL
     EAHYLQLFKN TVQFVTQKPL EVRFVNLNLE EPAAETNIQP VSETQTQNFS PSPSKQQPPN
     QAGTPQPNVP LSPEPVKVSS AWIDDTQSIL NPKYVFETFV IGNSNRFAHA AALAVAEVPA
     KVYNPFFVYG GVGLGKTHLM HAIGHRIRHN HPNLKVLYIS SEKFTNELIN SIRDGNPESF
     RQKYRNIDVL LVDDIQFLSK KEHTQEEFFH TFNTLHEANK QIIISSDRPP REIPTLEDRL
     RSRFEWGLIT DIQAPDLETR IAILRKKAMV ENLNFPNDVM IYIASRIDNN IRELEGAFIR
     VMAYASLVNK PINIDLATEA LKEIFPYGKP KQVTMELIKE TVATYFKIKQ DDLTAKKRTR
     NVAYPRQIAM YLCREMTDTS LPRIGEVFGG RDHTTVIHAN DKISRERNED GKLQQTINEL
     IKRIENA
//
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