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Database: UniProt
Entry: A0A1G0X669_9BACT
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ID   A0A1G0X669_9BACT        Unreviewed;       464 AA.
AC   A0A1G0X669;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-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=A2523_16715 {ECO:0000313|EMBL:OGV29181.1};
OS   Ignavibacteria bacterium RIFOXYD12_FULL_36_8.
OC   Bacteria; Ignavibacteriae; Ignavibacteria.
OX   NCBI_TaxID=1798454 {ECO:0000313|EMBL:OGV29181.1, ECO:0000313|Proteomes:UP000177243};
RN   [1] {ECO:0000313|EMBL:OGV29181.1, ECO:0000313|Proteomes:UP000177243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U.,
RA   Brodie E.L., Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected
RT   biogeochemical processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGV29181.1}.
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DR   EMBL; MHBA01000097; OGV29181.1; -; Genomic_DNA.
DR   Proteomes; UP000177243; 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:UP000177243};
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:UP000177243}.
FT   DOMAIN      158    289       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      369    438       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     166    173       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      438    458       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   464 AA;  52705 MW;  069994E203026106 CRC64;
     MLNIGLISKA PPKNLIEIWG DFLKEIKGNV TQMTFNTWFL PIKPLELSNS TIKVQLPSQF
     FWEWIDEHYK SLISKTMQNV LGEQISLTYV ISEEVEPKKT EKEIAPQVIE NTKPVPPKQE
     HNAFLNYRYT FDNFIKGENN QLARAAATAI SENPGGTSFN PLFLYGGVGL GKTHLMQAIG
     NKILEKIPDK RVIYLPSDIF TVQFVESIKS DKVNEFSGFY RSMDVLIIDD IQFLIGKEKT
     QDLFFHIFNT LHQARKQIVL SSDKPPKDLK GLDERLISRF QWGLSADIQS PDLETRIAIL
     KKKSEDYGML VSDEILEYIA NSITSNIREL EGCLIKLLAN SSLNSKDINL DLAKRTVKEI
     ATDRKINISI DNITKTVCSA LSVDENKLRD KTRKKEIVLA RQLAMFFSKE LTKSSLKTIG
     LHFGGRDHST VIHSCNSIEQ MQQEDSSIKT LVENLRSQIE LACS
//
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