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Database: UniProt
Entry: A0A0J6RFE8_9RHIZ
LinkDB: A0A0J6RFE8_9RHIZ
Original site: A0A0J6RFE8_9RHIZ 
ID   A0A0J6RFE8_9RHIZ        Unreviewed;       496 AA.
AC   A0A0J6RFE8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   25-OCT-2017, entry version 17.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=QR78_11230 {ECO:0000313|EMBL:KMO20114.1};
OS   Methylobacterium indicum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=1775910 {ECO:0000313|EMBL:KMO20114.1, ECO:0000313|Proteomes:UP000036498};
RN   [1] {ECO:0000313|EMBL:KMO20114.1, ECO:0000313|Proteomes:UP000036498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE2.11 {ECO:0000313|EMBL:KMO20114.1,
RC   ECO:0000313|Proteomes:UP000036498};
RA   Chaudhry V., Patil P.B.;
RT   "Comparative genomics of Methylobacterium species.";
RL   Submitted (NOV-2014) 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:SAAS00724167}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00911680}.
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:KMO20114.1}.
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DR   EMBL; JTHF01000091; KMO20114.1; -; Genomic_DNA.
DR   RefSeq; WP_048427600.1; NZ_JTHG01000233.1.
DR   EnsemblBacteria; KMO20114; KMO20114; QR78_11230.
DR   PATRIC; fig|427683.4.peg.2748; -.
DR   Proteomes; UP000036498; 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   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; 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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000036498};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036498}.
FT   DOMAIN      190    319       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      404    473       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     198    205       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   496 AA;  53353 MW;  49FD1138EAD5D283 CRC64;
     MRVDGSLAEG VGSGRGGNGE TAAADISGAW QRVKRRLRAE LGEDVFASWF ARLELQEVSG
     GVARLTVPTR FLKSWIESHY IDRVLATFRS EADGIESLEV GVRGAMAPAR PGAAAAAKPA
     PAPRPAASAG PANDLPEPER LARGPAPEGD LGGAPLDARL TFESFVVGRS NALAHAAAER
     VARHDGGPAL YNPLYFHAGV GLGKTHLLHG IGHAVKNAGR RVIYLTADRF MYGFVNALKT
     QSALAFKEKL RAIDVLILDD VQFIQGRSIQ AEFGHTLNAL IDAGRQVVVA ADRPPTELEA
     LDERVRSRLA GGLVVEIGTL DEALRASILQ SRLEAVRASH PAFEVGPAVA EYVAKAITAN
     GRDLEGAVNR LLAHATLTGA PVTLDTAETA IRDLVKNREP KRVKIEDIQK LVASRYNVSR
     SDILSERRTA AVVKPRQIAM YLSKVLTLRS LPEIGRRFGG RDHTTVLHAV RKIEKAIGED
     TALCDEVELL KRMLQD
//
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