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Database: UniProt
Entry: A0A0Q9KNP9_9MICO
LinkDB: A0A0Q9KNP9_9MICO
Original site: A0A0Q9KNP9_9MICO 
ID   A0A0Q9KNP9_9MICO        Unreviewed;       515 AA.
AC   A0A0Q9KNP9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, 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};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=ASG74_10850 {ECO:0000313|EMBL:KRE43130.1};
OS   Knoellia sp. Soil729.
OC   Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; Knoellia.
OX   NCBI_TaxID=1736394 {ECO:0000313|EMBL:KRE43130.1, ECO:0000313|Proteomes:UP000051965};
RN   [1] {ECO:0000313|EMBL:KRE43130.1, ECO:0000313|Proteomes:UP000051965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil729 {ECO:0000313|EMBL:KRE43130.1,
RC   ECO:0000313|Proteomes:UP000051965};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE43130.1, ECO:0000313|Proteomes:UP000051965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil729 {ECO:0000313|EMBL:KRE43130.1,
RC   ECO:0000313|Proteomes:UP000051965};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KRE43130.1}.
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DR   EMBL; LMSA01000002; KRE43130.1; -; Genomic_DNA.
DR   RefSeq; WP_056143522.1; NZ_LMSA01000002.1.
DR   EnsemblBacteria; KRE43130; KRE43130; ASG74_10850.
DR   Proteomes; UP000051965; 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:UP000051965};
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:UP000051965}.
FT   DOMAIN      208    336       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      420    489       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     216    223       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   515 AA;  57317 MW;  7943105D92FB2565 CRC64;
     MDQIWRTTLD ALDSDGIPVQ QRAFLSLAKL VGLLDETALI AVPNDFTKDI VETRLRDRVT
     ETLRSQLGHD VRLAVTVDPS LGDAPVLVPA GDADLVAAPH AAGPPGPAPT SATEPAPTDG
     DGRRAERRAE LDGIALVEDD EDERRDHASV ARTRSPGALR PRPGATVPEQ VELTRLNPKY
     TFDTFVIGAS NRFANAAALA VAETPAKAYN PLFIYGESGL GKTHLLHAIG HYARNLFPHV
     KVRYVNSEEF TNDFINSIRD DKAANFQRRY RDVDVLLIDD IQFLQGKVQT QEEFFHTFNT
     LHNANKQVVI TSDLPPKLLS GFEERMRSRF EWGLMTDVQP PDLETRIAIL RKKAAQERLS
     VPDDVLEFIA SRITTNIREL EGALIRVTAF ASLNRQPVDI SLAEIVLKDL IPHDSANQIT
     SATIMAQTAA YFGLTLEDLQ GQSRSRVLVT ARQIAMYLCR ELTDLSLPKI GQQFGGRDHT
     TVMHADKKIR QLMAERRAIY NQVTELTNRI KQQSR
//
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