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Database: UniProt
Entry: A0A1Q3WJR3_9BACT
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ID   A0A1Q3WJR3_9BACT        Unreviewed;       469 AA.
AC   A0A1Q3WJR3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   13-FEB-2019, entry version 16.
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=BGO59_18075 {ECO:0000313|EMBL:OJW75200.1};
OS   Spirosoma sp. 48-14.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC   Spirosoma.
OX   NCBI_TaxID=1895854 {ECO:0000313|EMBL:OJW75200.1, ECO:0000313|Proteomes:UP000186057};
RN   [1] {ECO:0000313|EMBL:OJW75200.1, ECO:0000313|Proteomes:UP000186057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=48-14 {ECO:0000313|EMBL:OJW75200.1};
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:OJW75200.1}.
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DR   EMBL; MKUD01000037; OJW75200.1; -; Genomic_DNA.
DR   Proteomes; UP000186057; 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; 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   Complete proteome {ECO:0000313|Proteomes:UP000186057};
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:UP000186057}.
FT   DOMAIN      167    297       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      378    447       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     175    182       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      447    469       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   469 AA;  53434 MW;  FFDDBD9FCF03BCB2 CRC64;
     MQREVTTVWN RCLNVIREIV PEQSFNTWFE PIVPLRLNGN VLTIQVPSEF FYEWLEENFV
     HALRKALDTA IGPTGQLEYS IIVDKGNEQN RPLTVNVPTT KSPQTAKPDN VNPDILKSPF
     QLKDLDSLTL DSYLNPSYTF ENYVEGDCNR LARSAGYAVA ERPGVTSFNP LMIYGGVGLG
     KTHLVQAIGN YIKNNSHNKF VLYVTSEKFT NQFLNAVRTD GIRDFTSFYM QVDVLVIDDV
     QFLQKKEKTQ EIFFHIFNHL HQSGKQIIMT SDRAPRALDG LEDRLLSRFK WGLSADLQTP
     DLETRIAIIQ KKLQTEGIYI DDNVIEYLAH SVNTNVRELE GVIVSLMAQA SLNRRDIDLE
     LAKQTLRNIV VDSDREVTID SVQEAVADYF NVTIADLKAK SRKRELVHPR QVAMYLAKEK
     TDLSLKSIGY HFGGRDHSTV IHAIQTISDL VAKHAETRDM IEKLKAQFK
//
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