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Database: UniProt
Entry: D9RYX0_THEOJ
LinkDB: D9RYX0_THEOJ
Original site: D9RYX0_THEOJ 
ID   D9RYX0_THEOJ            Unreviewed;       449 AA.
AC   D9RYX0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   16-JAN-2019, entry version 62.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:ADL06798.1};
GN   OrderedLocusNames=Toce_0001 {ECO:0000313|EMBL:ADL06798.1};
OS   Thermosediminibacter oceani (strain ATCC BAA-1034 / DSM 16646 /
OS   JW/IW-1228P).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis;
OC   Thermosediminibacter.
OX   NCBI_TaxID=555079 {ECO:0000313|EMBL:ADL06798.1, ECO:0000313|Proteomes:UP000000272};
RN   [1] {ECO:0000313|EMBL:ADL06798.1, ECO:0000313|Proteomes:UP000000272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1034 / DSM 16646 / JW/IW-1228P
RC   {ECO:0000313|Proteomes:UP000000272};
RX   PubMed=21304740;
RA   Pitluck S., Yasawong M., Munk C., Nolan M., Lapidus A., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Bruce D., Detter C.,
RA   Tapia R., Han C., Goodwin L., Liolios K., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Rohde M., Spring S., Sikorski J., Goker M.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Thermosediminibacter oceani type strain
RT   (JW/IW-1228P).";
RL   Stand. Genomic Sci. 3:108-116(2010).
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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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; CP002131; ADL06798.1; -; Genomic_DNA.
DR   RefSeq; WP_013274850.1; NC_014377.1.
DR   STRING; 555079.Toce_0001; -.
DR   EnsemblBacteria; ADL06798; ADL06798; Toce_0001.
DR   KEGG; toc:Toce_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; 219876at2; -.
DR   BioCyc; TOCE555079:G1GMA-1-MONOMER; -.
DR   Proteomes; UP000000272; 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   Gene3D; 3.30.300.180; -; 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; IPR038454; DnaA_N_sf.
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   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:SAAS00756129};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000272};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000272}.
FT   DOMAIN      144    272       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      356    425       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     152    159       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   449 AA;  50975 MW;  5E86D3EA6D392A0D CRC64;
     MTHNLPDLWQ QVLKTLGSEL NNDVSFNTFL KPTKLVSIED DIAIVEVPNE FLKGILEKRY
     ANLLKDILGS ILNRSVSIFF KIDPLASEEQ ASTVDTAEKD IKPVAEEGQS TLNSKYTFDT
     FVVGNSNRFA HAASLAVAQA PAKAYNPFFI YGGVGLGKTH LMHAIGHYIL QHNPSCKVVY
     VSSEKFTNEL INSIRDDKNV EFRNKYRNID VLLIDDIQFI AGKERTQEEF FHTFNALYEA
     NKQIIISSDR PPKEIPTLEE RLRSRFEWGL ITDIQPPDFE TRIAILRKKA MMENLTVPDD
     VINFIATKIE TNIRELEGAL IRIVAFSSLT NKPIDLDLAE HVLKDLLPNN KPKTVTVMDI
     LQVVGGHFSI KIDDFKSKKR TKELAYARQI AMYLCRELTD YSLPKIGEEF GGRDHTTVLH
     ACEKISRDIQ RDAQLSSLIE NLKKKILHG
//
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