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Database: UniProt
Entry: A0A2A1ZTJ9_9BACT
LinkDB: A0A2A1ZTJ9_9BACT
Original site: A0A2A1ZTJ9_9BACT 
ID   A0A2A1ZTJ9_9BACT        Unreviewed;       469 AA.
AC   A0A2A1ZTJ9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   16-JAN-2019, entry version 9.
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=CI105_01405 {ECO:0000313|EMBL:PAT02642.1};
OS   Candidatus Izimaplasma sp. ZiA1.
OC   Bacteria; Tenericutes; Candidatus Izimaplasma.
OX   NCBI_TaxID=2024899 {ECO:0000313|EMBL:PAT02642.1};
RN   [1] {ECO:0000313|EMBL:PAT02642.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZiA1 {ECO:0000313|EMBL:PAT02642.1};
RA   Kim S.-J., Rhee S.-K.;
RT   "Direct submision.";
RL   Submitted (AUG-2017) 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:PAT02642.1}.
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DR   EMBL; NQYJ01000001; PAT02642.1; -; Genomic_DNA.
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   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}.
FT   DOMAIN      157    288       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      376    445       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     165    172       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   469 AA;  54947 MW;  019AEFC934A4878F CRC64;
     MLYYFYDNEV NNMEKFTQIW EEIKIKLEED LDNQVFAELI NPVETVFKVV NNYVYLVVPN
     DFVKKRIELL YLNKLNRYLS SYVEETHKFK IITIEQAEKE LQDKKDFVIN EPESDINSKY
     LKGNLNLSYS FDSFVVGNSN RLAYTSATKV ADQPGIVANP LYIFGDVGLG KTHLMQCVGN
     YILEGDINKK VLYIKTDQFV EEYVRLASKR KFDEFNEKYR DVDVLLVDDI QFLAKKDKSQ
     LEFFKLFEHL HGQQKQIVIT SDRSASDLKD IMSRLTSRFE WGVTVDINRP DLEHRIKILE
     KKLTAETSDK DLIPKDVIEY IASVFDNNVR ELEGALKRVM FYCTAFNIDF TVKNAEIALH
     SLIKPKSTDK YMNNDKINNV LSVVSDYYRI STADLVSKKR TRKHVFPRQV AMYLIKQIYD
     LPYKKIGTFF NNRDHSTVMH SVEKINNEIQ MDINVKKDVE KLKIKCGEN
//
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