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Database: UniProt
Entry: A0A2G1ZSE1_9COXI
LinkDB: A0A2G1ZSE1_9COXI
Original site: A0A2G1ZSE1_9COXI 
ID   A0A2G1ZSE1_9COXI        Unreviewed;       456 AA.
AC   A0A2G1ZSE1;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   16-JAN-2019, entry version 9.
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   ORFNames=COB66_08425 {ECO:0000313|EMBL:PHQ78677.1};
OS   Coxiella sp. (in: Bacteria).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Coxiellaceae; Coxiella.
OX   NCBI_TaxID=59288 {ECO:0000313|EMBL:PHQ78677.1};
RN   [1] {ECO:0000313|EMBL:PHQ78677.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NORP135 {ECO:0000313|EMBL:PHQ78677.1};
RX   PubMed=29099490; DOI=.1038/ismej.2017.187;
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy
RT   inhabits the cold, oxic subseafloor aquifer.";
RL   ISME J. 12:1-16(2018).
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}.
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:PHQ78677.1}.
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DR   EMBL; NVSS01000150; PHQ78677.1; -; Genomic_DNA.
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   Coiled coil {ECO:0000256|SAM:Coils};
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}.
FT   DOMAIN      153    366       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      364    433       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     161    168       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      315    335       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   456 AA;  51625 MW;  D8BE1FBFC2AC19F1 CRC64;
     MADISTELSL WEKCLNYLKD EIPEKKFNTW IRPLHAEMQQ DGLSLLAPNK FVKEYISDNF
     LATIQSALSE LTNNAAPRIK LAIGTRLNAA QADQAPVQQR SIRKKITHPI SFGSTAAKSN
     VNRQFTFDNF VIGKSNQLAH AATLQVAQNP GQTYNPLFIY GGVGLGKTHL MHALGNHILA
     QNPEARIMYL HSERFVADMI KALQRNAMND FKKFYRGMNA LLIDDIQFFA GKERSQEEFF
     HTFNSLLDGQ QQIVLTCDRY PKEIKGLEER LQSRFGWGLT IAVEPPELET RVAILLSKAE
     RANVILPNEV AFFIAKHIQS NVRELEGALK RVIANAHFTG EPITVEFTRE ALKDLLTLQA
     KLVTVDNIQR TVADFYKIKL TDILSKRRSR SIARPRQMAM ALSKELTNHS LPEIGDAFGG
     RDHTTVLHAV RKIKELREES IALKDDWKNL LRILSA
//
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