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Database: UniProt
Entry: A0A0T0M7F1_9FLAO
LinkDB: A0A0T0M7F1_9FLAO
Original site: A0A0T0M7F1_9FLAO 
ID   A0A0T0M7F1_9FLAO        Unreviewed;       484 AA.
AC   A0A0T0M7F1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   16-JAN-2019, entry version 23.
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=ASG21_07015 {ECO:0000313|EMBL:KQS92191.1};
OS   Chryseobacterium sp. Leaf394.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Chryseobacterium.
OX   NCBI_TaxID=1736361 {ECO:0000313|EMBL:KQS92191.1, ECO:0000313|Proteomes:UP000051822};
RN   [1] {ECO:0000313|EMBL:KQS92191.1, ECO:0000313|Proteomes:UP000051822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf394 {ECO:0000313|EMBL:KQS92191.1,
RC   ECO:0000313|Proteomes:UP000051822};
RX   PubMed=26633631; DOI=.1038/nature16192;
RA   Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E.,
RA   Rott M., Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M.,
RA   Huttel B., McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL   Nature 528:364-369(2015).
RN   [2] {ECO:0000313|Proteomes:UP000051822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf394 {ECO:0000313|Proteomes:UP000051822};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000051822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf394 {ECO:0000313|Proteomes:UP000051822};
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: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:KQS92191.1}.
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DR   EMBL; LMQH01000011; KQS92191.1; -; Genomic_DNA.
DR   RefSeq; WP_056078984.1; NZ_LMQH01000011.1.
DR   EnsemblBacteria; KQS92191; KQS92191; ASG21_07015.
DR   Proteomes; UP000051822; 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:UP000051822};
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}.
FT   DOMAIN      181    312       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      392    461       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     189    196       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   484 AA;  54920 MW;  50D617B4806E4E41 CRC64;
     MKENLMMTWQ NCLQFMRDNL NAAEDNSDLK KLEKSFDLLF DKVQPVSLVD NNLTLMVPSD
     FYKEYIEDNY LSLLSAALKK YIGKGVKLWY SVMENKPAGQ EKPVTMNMKG KTVATPKVQE
     TMPQGFSGNI VNPFVVPGIK KVNIDSNLKA DFSFDNYVEG ESNKFASTVA KSIAKRPGAT
     AFNPLFLYGG YGVGKTHLGQ AVGLEVKSQF PDKVVLYLSS EKFIQQFISA AKAHKQTEFA
     NFYQMVDVLI IDDIQFLSGK SATQDSFFHI FDYLHQNGKQ IILTSDKAPV DIMDIQDRIV
     SRFKWGLSAE IKSPDLETRK QIIVDKLSRD GIVLTDDMLD FLASEVKTNV RELIGVINSV
     IAYSTIYKSD LSLELLKETI NKIAANQKKI INIPYIQEVV CDYFGIKREQ LLSKTRKREI
     ALPRQLAMYF AKEYTNSTFT KIGEEMGGKD HSTVMYACET IKDVSKIDKE VKKYVKDLTE
     RIKH
//
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