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Database: UniProt
Entry: A0A1A5TAW5_9RHIZ
LinkDB: A0A1A5TAW5_9RHIZ
Original site: A0A1A5TAW5_9RHIZ 
ID   A0A1A5TAW5_9RHIZ        Unreviewed;       514 AA.
AC   A0A1A5TAW5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   13-FEB-2019, entry version 22.
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=A9K68_00525 {ECO:0000313|EMBL:OBR01632.1};
OS   Mesorhizobium sp. AA22.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=1854057 {ECO:0000313|EMBL:OBR01632.1, ECO:0000313|Proteomes:UP000093625};
RN   [1] {ECO:0000313|EMBL:OBR01632.1, ECO:0000313|Proteomes:UP000093625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AA22 {ECO:0000313|EMBL:OBR01632.1,
RC   ECO:0000313|Proteomes:UP000093625};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) 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:OBR01632.1}.
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DR   EMBL; LYTO01000001; OBR01632.1; -; Genomic_DNA.
DR   RefSeq; WP_065005875.1; NZ_LYTO01000001.1.
DR   EnsemblBacteria; OBR01632; OBR01632; A9K68_00525.
DR   OrthoDB; 219876at2; -.
DR   BioCyc; GCF_001672375:A9K68_RS00520-MONOMER; -.
DR   Proteomes; UP000093625; 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   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   Complete proteome {ECO:0000313|Proteomes:UP000093625};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093625}.
FT   DOMAIN      205    332       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      420    489       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     213    220       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   514 AA;  57462 MW;  1F547CFAC7538B6E CRC64;
     MQSGIERELT GDLPFPGTLT EGDDMSASID AEQKFDRVKA QLKARLGTEV YSSWFGRMKV
     AEASRGIVRI SVPTAFLRSW INGHYLDLIA ELWKHEDPEI LKIEIVVRTA TRPGRNGVEP
     EVAPARKMTR QAQTALAAGT ASPGRLERVP APRPGTPAET EFRHNVLGSP LDPRYTFGSF
     IEGPSNRVAF AAAKAVAESQ SSAVRFNPLF LHATVGLGKT HLLQAIAAES LKQNPKSRVV
     YLTAEYFMWR FATAIRDNNA LTLKEQLRDI DLLIIDDMQF LQGKSIQHEF CHLINMLLDS
     AKQVVVAADR PPSELESLEP RVRSRLNGGV ALEMSAPDFA MRIGMLKLRL ATAKADDASL
     DISDEILNHV ARTVTGSGRE LEGAFNQLLF RQSFEPQITI DRIDEILGHI YRSGEPKRVR
     IEDIQRIVAR HYNVSKTELL SNRRTRTIVK PRQVAMYLSK VMTPRSLPEI GRRFGGRDHT
     TVLHAVRKIE DLSGVDNTLA QELELLRRLI NDQA
//
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