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Database: UniProt
Entry: A0A1M3M9R7_9BACT
LinkDB: A0A1M3M9R7_9BACT
Original site: A0A1M3M9R7_9BACT 
ID   A0A1M3M9R7_9BACT        Unreviewed;       466 AA.
AC   A0A1M3M9R7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   16-JAN-2019, entry version 14.
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=BGP01_09185 {ECO:0000313|EMBL:OJX88507.1};
OS   Paludibacter sp. 47-17.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Paludibacteraceae; Paludibacter.
OX   NCBI_TaxID=1895899 {ECO:0000313|EMBL:OJX88507.1, ECO:0000313|Proteomes:UP000183960};
RN   [1] {ECO:0000313|EMBL:OJX88507.1, ECO:0000313|Proteomes:UP000183960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47-17 {ECO:0000313|EMBL:OJX88507.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T.,
RA   Anantharaman K., Tringe S., Hettich R.L., Harrison S.T.,
RA   Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process
RT   performance in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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: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:OJX88507.1}.
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DR   EMBL; MKVT01000020; OJX88507.1; -; Genomic_DNA.
DR   Proteomes; UP000183960; 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   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; IPR025662; Sigma_54_int_dom_ATP-bd_1.
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.
DR   PROSITE; PS00675; SIGMA54_INTERACT_1; 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:UP000183960};
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:UP000183960}.
FT   DOMAIN      163    371       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      374    443       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     171    178       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   466 AA;  52809 MW;  8DD234908653BD90 CRC64;
     MMSHSPEKLW SKCLEVIKDN INEASFNTWF MPIVPLQYDN NVLVLQVPSQ YFVEFIEEKY
     IDLLRKTLYR VLGEGTLLEY RVLIDKTSGQ GTRIPSEGNH PRPAAAPAGA APRYVDPYQK
     QRLPEIDPQL NLKYNFNNLV EGKSNKLART AGMSIANDPG KTIFNPLFVY GESGVGKTHL
     ANAIGVLTKQ LHPDKRVLYV SANTFLIQYT DAVRRNAAND FLNFYQTIDV LILEDIQEMM
     GKTGTQNTFF HLFNHLHQNG KQLIITSDRS PLVLAGMEQR LLTRFKWGLS AEIEKPDSEL
     RKAILKNKIY RDGLEISDEV VDFIATHVTD NVRDLEGTLA SLLAHSTLAN MPIDMHLAER
     VVGRIVNIKP RATTVEQIRD LVCEHFSLSV DAISTRSRKR EVVQARQIAM YLSKHHTKNS
     LSSIGDLIGQ RDHATVLHAC KIVTDLMEID KSFRMSVKEI EQKLKA
//
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