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Database: UniProt
Entry: A0A563CKV6_9BACT
LinkDB: A0A563CKV6_9BACT
Original site: A0A563CKV6_9BACT 
ID   A0A563CKV6_9BACT        Unreviewed;       451 AA.
AC   A0A563CKV6;
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:TWP15128.1};
GN   ORFNames=EUA74_03065 {ECO:0000313|EMBL:TWP15128.1};
OS   TM7 phylum sp. oral taxon 352.
OC   Bacteria; Candidatus Saccharibacteria.
OX   NCBI_TaxID=713054 {ECO:0000313|EMBL:TWP15128.1, ECO:0000313|Proteomes:UP000319173};
RN   [1] {ECO:0000313|EMBL:TWP15128.1, ECO:0000313|Proteomes:UP000319173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM7_HOT_352-SAG8 {ECO:0000313|EMBL:TWP15128.1,
RC   ECO:0000313|Proteomes:UP000319173};
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:TWP15128.1}.
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DR   EMBL; SDRM01000012; TWP15128.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A563CKV6; -.
DR   OrthoDB; 9807019at2; -.
DR   Proteomes; UP000319173; 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; 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.
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}.
FT   DOMAIN          148..278
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          358..427
FT                   /note="Chromosomal replication initiator DnaA C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00760"
FT   REGION          76..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         156..163
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   451 AA;  51300 MW;  58282A60AA37B934 CRC64;
     MDSHAVWQGV LGEIEVTVSS SSFTAWFKNT KLEIISDKEV LIIAPNIFAR TQLEKRFHPQ
     ILEALAHNGI NAPSISYNVE SSNKKPRVNR EVDKSGQQET AKPLILPSRK SHSSNLNPRY
     TFDNFIVGSS NDLAYAACQA VAAHPGEKYN PLYLYGGSGL GKTHLMQAVG NEIVKKQSSA
     RVLYITTETF VNEFLDSIRF KKKGFSDKYR NVDVLIVDDM QFIAGKEKTQ DEFFHTFNDL
     HQNNKQIIIS SDKPPKSIPT LTDRLRSRFE WGMAIDIQMP DYETRCAIVK AKAELSNTEL
     DSDVVEYLAT NFKTNIRELE GALNRLLAYA EMQNFTPDLV AAEGILGDIK RNRPQHITAK
     QIIDKTARYY NIDVKDMCSS RRDKFIAMPR QIAMFLLRSE LKMSFPKIAQ ELGRKDHTTA
     MHSIEKITKE SLTNVSIREQ INDIKDKLYV H
//
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