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Database: UniProt
Entry: A0A563C7Y3_9BACT
LinkDB: A0A563C7Y3_9BACT
Original site: A0A563C7Y3_9BACT 
ID   A0A563C7Y3_9BACT        Unreviewed;       463 AA.
AC   A0A563C7Y3;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   08-NOV-2023, entry version 15.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:TWP13997.1};
GN   ORFNames=EUA77_01875 {ECO:0000313|EMBL:TWP13997.1};
OS   TM7 phylum sp. oral taxon 351.
OC   Bacteria; Candidatus Saccharibacteria.
OX   NCBI_TaxID=713053 {ECO:0000313|EMBL:TWP13997.1, ECO:0000313|Proteomes:UP000319745};
RN   [1] {ECO:0000313|EMBL:TWP13997.1, ECO:0000313|Proteomes:UP000319745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM7_HOT_351-SAG1 {ECO:0000313|EMBL:TWP13997.1,
RC   ECO:0000313|Proteomes:UP000319745};
RA   Cross K.L., Podar M.;
RT   "Targeted isolation and cultivation of microbial dark matter through
RT   reverse genomics.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in the initiation and regulation of
CC       chromosomal replication. Binds to the origin of replication; it binds
CC       specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-
CC       TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
CC       {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00377}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|ARBA:ARBA00006583,
CC       ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU004227}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TWP13997.1}.
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DR   EMBL; SDRJ01000012; TWP13997.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A563C7Y3; -.
DR   Proteomes; UP000319745; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; cd00009; AAA; 1.
DR   CDD; cd06571; Bac_DnaA_C; 1.
DR   Gene3D; 1.10.1750.10; -; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.30.300.180; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00362; DnaA; 1.
DR   PANTHER; PTHR30050; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 1.
DR   PANTHER; PTHR30050:SF2; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48295; TrpR-like; 1.
DR   PROSITE; PS01008; DNAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00377};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00377};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00377};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00377};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00377}; Reference proteome {ECO:0000313|Proteomes:UP000319745}.
FT   DOMAIN          159..293
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          371..440
FT                   /note="Chromosomal replication initiator DnaA C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00760"
FT   BINDING         167..174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   463 AA;  52340 MW;  2FC9907EABEE1B9F CRC64;
     MEVVAVFDVW NNVLAELEQK ISQENYATFF AQTNTSLIST DDGMIQIGVP NIFMQANIRK
     KFDQQIRDAL ISNKISVKNT NYVIVNNATR VKKPREVVLE DLQTRVNTVE KIKIPTNNFN
     PTLLTGLNNK FTMDNFVVGT NNELAVAVAK NIIENPGDKY NPFFLYGGPG LGKTHLVEAI
     GNELLKRNPK LRILYTPINH FYSDFITAVR KGDMENFHKK FQKLDVLIID DFQFIVGKEK
     SQEEFFNIFN DMHQANKQVI ITSDRLPSQI KTVDERLASR LTMTGAFDLQ YPTFEDRCAI
     LHAKAEFDGV DVENQAIEYI AKNVETNIRD LQSLYGKIIA LSELKGVSPL TIIQDGLASI
     STGGVRSRNL TPKTIVGKVS DYYNITPDEL CGKSRVSNIK TARQVAMFLM SKDLQMSTPK
     IALEVGVKDH TTVMHGIKKI ESDMKLNFSL RDEISEIREQ LSE
//
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