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Database: UniProt
Entry: A0A6I5XAL5_9MICO
LinkDB: A0A6I5XAL5_9MICO
Original site: A0A6I5XAL5_9MICO 
ID   A0A6I5XAL5_9MICO        Unreviewed;       502 AA.
AC   A0A6I5XAL5;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   12-AUG-2020, sequence version 1.
DT   08-NOV-2023, entry version 13.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|ARBA:ARBA00018893, ECO:0000256|HAMAP-Rule:MF_00377};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:QGN58644.1};
GN   ORFNames=GKE56_13015 {ECO:0000313|EMBL:QGN58644.1};
OS   Tetrasphaera sp. HKS02.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Tetrasphaera.
OX   NCBI_TaxID=1813880 {ECO:0000313|EMBL:QGN58644.1, ECO:0000313|Proteomes:UP000423741};
RN   [1] {ECO:0000313|EMBL:QGN58644.1, ECO:0000313|Proteomes:UP000423741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKS02 {ECO:0000313|EMBL:QGN58644.1,
RC   ECO:0000313|Proteomes:UP000423741};
RA   Im W.-T.;
RT   "Complete genome sequence of Tetrasphaera sp. HKS02.";
RL   Submitted (NOV-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}.
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DR   EMBL; CP046121; QGN58644.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6I5XAL5; -.
DR   KEGG; teh:GKE56_13015; -.
DR   OrthoDB; 9807019at2; -.
DR   Proteomes; UP000423741; Chromosome.
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; 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   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:UP000423741}.
FT   DOMAIN          195..325
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          407..476
FT                   /note="Chromosomal replication initiator DnaA C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00760"
FT   REGION          93..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         203..210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   502 AA;  55680 MW;  3A12AA64CB495D02 CRC64;
     MSDADLDFAQ IWQNTISTLD ADGLPARERA FLTLARFSGL LDGTALIKVP NDYTKDVVET
     RVRDEVTHAL SSQLGTTVHL AVTVDLSLEE GHLDQDTDGL DEGSGGPSGT GAPSGHQGGP
     GLSGLSTAPA QPDNVYPMAR HAETQRRPRD EVPSITDESA TRLNPKYTFD TFVIGASNRF
     AHAAAVAVAE APAKAYNPLF VYGESGLGKT HLLHAIGHYA RNLYPHVKVR YVNSEEFTND
     FINSIRDDKA SNFQRRYRDV DVLLIDDIQF LQGKVQTQEE FFHTFNTLHN ANKQVVITSD
     LPPKLLSGFE ERMRSRFEWG LLTDVQPPDL ETRIAILRKK AIQEKMSAPD EVLEFIASRI
     STNIRELEGA LIRVTAFASL NRQSVDMGLA EIVLKDLIPN EQGSQITSAT IMAQTAAYFG
     LTIEDLCGSS RSRVLVTARQ IAMYLCRELT DLSLPKIGQQ FGGRDHTTVM HADKKIRQLM
     AERRAIYNQV TELTNRIKQQ SR
//
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