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Database: UniProt
Entry: A0A0M3QER3_9DELT
LinkDB: A0A0M3QER3_9DELT
Original site: A0A0M3QER3_9DELT 
ID   A0A0M3QER3_9DELT        Unreviewed;       452 AA.
AC   A0A0M3QER3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-SEP-2017, entry version 17.
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:ALC14803.1};
GN   ORFNames=DSOUD_0001 {ECO:0000313|EMBL:ALC14803.1};
OS   Desulfuromonas soudanensis.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Desulfuromonadaceae; Desulfuromonas.
OX   NCBI_TaxID=1603606 {ECO:0000313|EMBL:ALC14803.1, ECO:0000313|Proteomes:UP000057158};
RN   [1] {ECO:0000313|EMBL:ALC14803.1, ECO:0000313|Proteomes:UP000057158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WTL {ECO:0000313|EMBL:ALC14803.1,
RC   ECO:0000313|Proteomes:UP000057158};
RA   Badalamenti J.P., Summers Z.M., Gralnick J.A., Bond D.R.;
RT   "Isolation and Genomic Characterization of a Novel Halophilic Metal-
RT   Reducing Deltaproteobacterium from the Deep Subsurface.";
RL   Submitted (JUL-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}.
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DR   EMBL; CP010802; ALC14803.1; -; Genomic_DNA.
DR   RefSeq; WP_053549065.1; NZ_CP010802.1.
DR   EnsemblBacteria; ALC14803; ALC14803; DSOUD_0001.
DR   KEGG; des:DSOUD_0001; -.
DR   PATRIC; fig|1603606.3.peg.2; -.
DR   KO; K02313; -.
DR   Proteomes; UP000057158; Chromosome.
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:UP000057158};
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:UP000057158}.
FT   DOMAIN      149    277       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      360    429       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     157    164       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   452 AA;  51781 MW;  7A8CFF97FABEFAD5 CRC64;
     MNKLWQETLV HLEQALNPQH FTTWIKPIRF VSLKKDLIQL EVPNRFVLDW IRIHYSQLIQ
     ETLSNIGAVV YRIQFSIATQ NSDSILPENK LSPGINKNQQ EIKIEPQPRS CNYAFNLNSK
     YSFDEFVSGS SNQFAYAAAM AVANNPATTY NPLFIYGGVG LGKTHLVNAI GNAILRKNPD
     MKVCYYTSEK FMNELINSLR YAKMDEFRNK FRTMDVLLID DVQFIAGKER TQEEFFHTFN
     SLYESHKQIV VTSDKFPKEI PGLEERLRSR FEWGLIADIQ APDMETKHAI LKMKAEQNGI
     NLPEDVALFL ANSISSNVRE LEGFLVRIGA FASLTSTPVT LTMAREVLKD ILVEKNRELS
     IEEIQKVVAT YYNIKVSEIK SSRRLKVLVL PRQIAMYLSR QLTSYSYPEI GERFGGKDHS
     TIIHAIKKIE KAIENDYQLS ATINNIKNAL AH
//
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