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Database: UniProt
Entry: A0A2D8PDL7_9RHOB
LinkDB: A0A2D8PDL7_9RHOB
Original site: A0A2D8PDL7_9RHOB 
ID   A0A2D8PDL7_9RHOB        Unreviewed;       464 AA.
AC   A0A2D8PDL7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   16-JAN-2019, entry version 10.
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=CMH11_18905 {ECO:0000313|EMBL:MAM63557.1};
OS   Maritimibacter sp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Maritimibacter.
OX   NCBI_TaxID=2003363 {ECO:0000313|EMBL:MAM63557.1, ECO:0000313|Proteomes:UP000224593};
RN   [1] {ECO:0000313|Proteomes:UP000224593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Graham E.D., Heidelberg J.F.;
RT   "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from
RT   the Global Oceans.";
RL   Submitted (SEP-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:MAM63557.1}.
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DR   EMBL; NZNT01000029; MAM63557.1; -; Genomic_DNA.
DR   Proteomes; UP000224593; 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:UP000224593};
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:UP000224593}.
FT   DOMAIN      156    286       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      372    441       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     164    171       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   464 AA;  52312 MW;  034D4CC662498A4A CRC64;
     MVKQVKDEMT DTMWGQVRAQ LEKSVGQNNY RNWIEPLEFA DLEGGVATFL VPTNFMGTWV
     QRNFGEQILR HMISAGAKVS RLEFVVPASA PQARAATTGE TPPPANGNGR PARTGGGELP
     GAPLDKRFTF DNFVVGKPNE LAHAAARRVA EGGPVTFNPL FLYGGVGLGK THLMHAIAHE
     MQERNPDLRV VYLSAEQFMY RFVQALREKQ MMDFKHLFRS VDVLMVDDVQ FIAGKDSTQE
     EFFHTFNALV DQNKQIIISA DRAPGEIKDL EERIKSRLQC GLVVDLHPTD YELRLGVLQT
     KVAAYREQYP DLSIADGVLE FLAHRITTNV RVLEGALMRL FAFASLVGGE ITLERAQECL
     TDVLRASDRK VTVEEIQRKV AEHYGVRFSD MIGPKRLRSI ARPRQVAMML SKELTTRSYP
     DIGRRFGGRD HSTVMHAVKR VEELIKSDQQ IAEDVELLRR LLEH
//
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