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Database: UniProt
Entry: R7RUD5_9CLOT
LinkDB: R7RUD5_9CLOT
Original site: R7RUD5_9CLOT 
ID   R7RUD5_9CLOT            Unreviewed;       458 AA.
AC   R7RUD5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-SEP-2017, entry version 31.
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   ORFNames=TCEL_02028 {ECO:0000313|EMBL:CDF58960.1};
OS   Thermobrachium celere DSM 8682.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Thermobrachium.
OX   NCBI_TaxID=941824 {ECO:0000313|EMBL:CDF58960.1, ECO:0000313|Proteomes:UP000014923};
RN   [1] {ECO:0000313|EMBL:CDF58960.1, ECO:0000313|Proteomes:UP000014923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8682 {ECO:0000313|EMBL:CDF58960.1,
RC   ECO:0000313|Proteomes:UP000014923};
RA   Ciranna A., Larjo A., Kivisto A., Santala V., Roos C., Karp M.;
RT   "Draft genome sequence of the hydrogen-ethanol-producing anaerobic
RT   alkalithermophilic Caloramator celere.";
RL   Submitted (MAR-2013) 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}.
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:CDF58960.1}.
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DR   EMBL; CAVN010000110; CDF58960.1; -; Genomic_DNA.
DR   RefSeq; WP_018664106.1; NZ_HF952022.1.
DR   EnsemblBacteria; CDF58960; CDF58960; TCEL_02028.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000014923; 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:UP000014923};
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:UP000014923}.
FT   DOMAIN      153    281       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      365    434       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     161    168       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   458 AA;  52477 MW;  2555F29B2EA5A7DD CRC64;
     MGTDIHSLWE KTLNIVKTEL TEVGFNTWIK SLKPIKLTND SFYLLAPTEF SKNILDARYK
     DLIGNAFKMV ASKKYEIKFV LETDDIFKEL DSNKEPQIKD EQDTPSSQPK QTNDELTTST
     LNPKYTFDTF VVGNSNRFAH AASLAVAEAP AKAYNPLFIY GGVGLGKTHL MHAIGHYILN
     NNPKARVVYV SSEKFTNELI NSIKDDKNVE FRNKYRNVDV LLIDDIQFIA GKERTQEEFF
     HTFNALYEAN KQIIISSDRP PKEIPTLEDR LRSRFEWGLI ADIQPPDFET RIAILKKKAD
     MENLQVPNEV MVYIANKIQS NIRELEGALI RIVAFASLSN KEISVELATD VLKDIISNKN
     NKQITVELIQ DVVASYYNLR IEDFKSKRRT KNVAYPRQIA MYLARKLTDL SLPKIGEEFG
     GRDHTTVIHA YEKISEDLEK DDALKETIDE LIKKINQK
//
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