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Database: UniProt
Entry: DNAA_DESRM
LinkDB: DNAA_DESRM
Original site: DNAA_DESRM 
ID   DNAA_DESRM              Reviewed;         441 AA.
AC   A4J0F0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   07-JUN-2017, entry version 67.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN   Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN   OrderedLocusNames=Dred_0001;
OS   Desulfotomaculum reducens (strain MI-1).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=349161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MI-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-2007) 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:0000255|HAMAP-Rule:MF_00377}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00377}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00377}.
DR   EMBL; CP000612; ABO48553.1; -; Genomic_DNA.
DR   RefSeq; WP_011876397.1; NC_009253.1.
DR   ProteinModelPortal; A4J0F0; -.
DR   SMR; A4J0F0; -.
DR   STRING; 349161.Dred_0001; -.
DR   EnsemblBacteria; ABO48553; ABO48553; Dred_0001.
DR   KEGG; drm:Dred_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000001556; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:InterPro.
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; Complete proteome; Cytoplasm; DNA replication;
KW   DNA-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    441       Chromosomal replication initiator protein
FT                                DnaA.
FT                                /FTId=PRO_1000072156.
FT   NP_BIND     144    151       ATP. {ECO:0000255|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   441 AA;  50668 MW;  BE5EEB0062A96F0B CRC64;
     MQNDVLARWE QVLIRLEKQV NKHSFETWLT KCKPVAFYDN TIIIEVPDHF SKSWLADRYA
     PIIKQAYESI MHQEISLQFI LAGQEVDQPK PKERSSEETY INILNPRYTF DTFVVGNSNR
     FAHAASLAVA ESPAKAYNPL FIYGGVGLGK THLMHAIGHY ILENNQNLKV AYVTSEKFTN
     ELINSIRDDQ TVEFRNKYRS MDILLIDDIQ FLEKKERTQE EFFHTFNTLY EANKQIIISS
     DRPPKEIATL EDRLRSRFEW GLITDMQSPD YETRVAILRK KAQLEAIKNI PDETIAYIAD
     KIQSNIRELE GALIRVSAFS SLEQRDATPQ LAAEVLKDVI APSKPKIITT PLIMQTVADF
     YGLRIEDLKA KKRTRSVAFP RQVAMYLARE LTDLSLPKIG DEFGGRDHTT VLHACDKITT
     DLSSDPVLQE TIKELKKRIG E
//
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