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Database: UniProt
Entry: A0A0G0Z4V9_9BACT
LinkDB: A0A0G0Z4V9_9BACT
Original site: A0A0G0Z4V9_9BACT 
ID   A0A0G0Z4V9_9BACT        Unreviewed;       452 AA.
AC   A0A0G0Z4V9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   25-OCT-2017, entry version 17.
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   ORFNames=UU61_C0007G0006 {ECO:0000313|EMBL:KKS08013.1};
OS   Parcubacteria group bacterium GW2011_GWB1_41_4.
OC   Bacteria; unclassified Parcubacteria group.
OX   NCBI_TaxID=1618867 {ECO:0000313|EMBL:KKS08013.1, ECO:0000313|Proteomes:UP000034734};
RN   [1] {ECO:0000313|EMBL:KKS08013.1, ECO:0000313|Proteomes:UP000034734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a
RT   large radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKS08013.1}.
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DR   EMBL; LCBH01000007; KKS08013.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKS08013; KKS08013; UU61_C0007G0006.
DR   PATRIC; fig|1618867.3.peg.135; -.
DR   Proteomes; UP000034734; 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:UP000034734};
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:UP000034734}.
FT   DOMAIN      148    280       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      359    428       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     156    163       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   452 AA;  51014 MW;  19E95FCA46AF42C6 CRC64;
     MDLKDIWQSV LNDIELNISR ASFITWFKNS SLIKKDGSTV VVACHNSFTK EWLENKYHKL
     ILKSLRNTNT EIKAVEYIVR VDVKPQIKNT PTKITISPES IPLELGGYAV DKETGLNLKY
     SFENFVVGSN NEVAYAAAQA SGENPGTAYN PLFVYGGVGL GKTHLLHALG NAIKNRFPKK
     KIKYTTAEKF LSDIVSSLRT KTIAELKDKF KNLDALLIDD IQFIAGAEKT QQELFHIFNA
     LYSHNKQIAF ASDRPPKAIA SIEERLRSRF EGGMTADIGL PDLETRIAIL KAKAQRENTL
     LNEKIIETIA KQVQKNIREL EGAFNRISAY IKVKGKEPTQ KEVESLLSDI SRSSTKTMTP
     KQLLKAVVDF YDLTEETILK KSRSQELVRP RQVAMYLMRE TLKMSFPNIG EKLGGKDHTT
     VIHACEKIEK ELVFDTQLAQ EINSIKEKIF AE
//
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