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Database: UniProt
Entry: A0A0T6A0A9_9BACT
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ID   A0A0T6A0A9_9BACT        Unreviewed;       447 AA.
AC   A0A0T6A0A9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   25-OCT-2017, entry version 13.
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   ECO:0000313|EMBL:KRT68515.1};
GN   ORFNames=XU15_C0020G0017 {ECO:0000313|EMBL:KRT68515.1};
OS   candidate division NC10 bacterium CSP1-5.
OC   Bacteria; candidate division NC10.
OX   NCBI_TaxID=1640516 {ECO:0000313|EMBL:KRT68515.1, ECO:0000313|Proteomes:UP000051123};
RN   [1] {ECO:0000313|EMBL:KRT68515.1, ECO:0000313|Proteomes:UP000051123}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSP1-5 {ECO:0000313|EMBL:KRT68515.1};
RA   Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA   Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT   "Critical biogeochemical functions in the subsurface are associated
RT   with bacteria from new phyla and little studied lineages.";
RL   Submitted (MAY-2015) 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:SAAS00911680}.
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:KRT68515.1}.
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DR   EMBL; LDXR01000020; KRT68515.1; -; Genomic_DNA.
DR   PATRIC; fig|1640516.3.peg.2548; -.
DR   Proteomes; UP000051123; 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: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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000051123};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051123}.
FT   DOMAIN      145    273       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      355    424       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     153    160       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   447 AA;  50749 MW;  65BA20BDA75D3D56 CRC64;
     MSGQSLMSQE VWQAAISNIQ RQLIPHSFAT WFRPLTLGTI HNNRLQILLP NRFFKEWFEE
     HYLEFLRSAL EDLLFTRVEI ELVVPEQDAS PPPPPKETPP KRTVRRSGPT TSLNAKYTFD
     SFVVGAGNQL AHAASLAIAE QISKVYNPLF VYGGVGLGKT HLLHAIGHLV LERDNLVRVS
     YVSSEKFTND LINAIRFDAT SEFRNRYRSV DVLLIDDIQF IAGKERTQEE FFHTFNDLYN
     ASKQIVLTSD SIPKEIPGLE ERLRSRFEWG LIADIQAPDM ETKAAILRKK AQAEGVQIPD
     EVSLFIASNV KSNVRELEGY LVRIVAYASL TNQAITLDLA REILKEFMNG DRAITIPRIL
     EVVSDFFRLN EKELLSRSRH KSIVLPRQVA MYLCRTQTNA SLPDIGAELG GKDHSTVIHA
     CAKVRELIAK DEKFRKQLHD LTNRLTG
//
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