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Database: UniProt
Entry: A0A0F0KNQ2_9MICO
LinkDB: A0A0F0KNQ2_9MICO
Original site: A0A0F0KNQ2_9MICO 
ID   A0A0F0KNQ2_9MICO        Unreviewed;       463 AA.
AC   A0A0F0KNQ2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   25-OCT-2017, entry version 24.
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:KJL21735.1};
GN   ORFNames=RN50_01633 {ECO:0000313|EMBL:KJL21735.1};
OS   Microbacterium foliorum.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=104336 {ECO:0000313|EMBL:KJL21735.1, ECO:0000313|Proteomes:UP000033572};
RN   [1] {ECO:0000313|EMBL:KJL21735.1, ECO:0000313|Proteomes:UP000033572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12966 {ECO:0000313|EMBL:KJL21735.1,
RC   ECO:0000313|Proteomes:UP000033572};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on
RT   heavy metal contaminated environments.";
RL   Submitted (FEB-2015) 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:SAAS00735475}.
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:KJL21735.1}.
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DR   EMBL; JYIU01000040; KJL21735.1; -; Genomic_DNA.
DR   RefSeq; WP_045254007.1; NZ_JYIU01000040.1.
DR   EnsemblBacteria; KJL21735; KJL21735; RN50_01633.
DR   GeneID; 31896051; -.
DR   PATRIC; fig|104336.4.peg.1676; -.
DR   Proteomes; UP000033572; 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; 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   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:UP000033572};
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:UP000033572}.
FT   DOMAIN      158    286       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      370    439       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     166    173       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   463 AA;  51929 MW;  82C37D2866D6BAE6 CRC64;
     MSSPAQPDVP IWTTVQELLE ADDRVTPQLQ GFLSLAVPAG VMAATLYLEV PNDLTAAQIN
     KRLRLPIMEA LSHIGEEVTS YRVVVNHELA EQPTAPIAVA DYGRQEQSRI ESPMEQPTQL
     RHESRLNPKY TFDNFVIGQS NRFAHAAAVA VAEAPAKAYN PLFIYGDSGL GKTHLLHAIG
     DYAQSLYAGV KVRYVSSEEF TNDFINSIAN NRGAAFQARY REVDILLIDD IQFLQGRAET
     QEAFFHTFNT LHDHNKQVVI TSDVAPKHLT GFEDRMRSRF EWGLITDVQA PDLETRIAIL
     RKKAQSEALH IPDEVLEYIA TVVSSNIREL EGALIRVSAF ASLNRSALDI SLAQTVLRDI
     IDTAEDNIIS PTDIITATAQ YFKLTVDDLY GSSRSQQIAT SRQIAMYLCR ERTSLSLPKI
     GQLFGNRDHT TVMYAYKKIS ELMKERRSIY NQVTEITTQL GRR
//
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