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Database: UniProt
Entry: A0A0Q6F8Y8_9ACTN
LinkDB: A0A0Q6F8Y8_9ACTN
Original site: A0A0Q6F8Y8_9ACTN 
ID   A0A0Q6F8Y8_9ACTN        Unreviewed;       498 AA.
AC   A0A0Q6F8Y8;
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=ASG49_14360 {ECO:0000313|EMBL:KQT90991.1};
OS   Marmoricola sp. Leaf446.
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Marmoricola.
OX   NCBI_TaxID=1736379 {ECO:0000313|EMBL:KQT90991.1, ECO:0000313|Proteomes:UP000051542};
RN   [1] {ECO:0000313|EMBL:KQT90991.1, ECO:0000313|Proteomes:UP000051542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf446 {ECO:0000313|EMBL:KQT90991.1,
RC   ECO:0000313|Proteomes:UP000051542};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT90991.1, ECO:0000313|Proteomes:UP000051542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf446 {ECO:0000313|EMBL:KQT90991.1,
RC   ECO:0000313|Proteomes:UP000051542};
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:KQT90991.1}.
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DR   EMBL; LMRF01000005; KQT90991.1; -; Genomic_DNA.
DR   EnsemblBacteria; KQT90991; KQT90991; ASG49_14360.
DR   Proteomes; UP000051542; 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:UP000051542};
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:UP000051542}.
FT   DOMAIN      189    317       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      401    470       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     197    204       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   498 AA;  56352 MW;  AFEA901BD727D47A CRC64;
     MVENLPPNQR MWLTTSQPLM LAENTAVVAV PNEFTRTQLE GRLRTRIEDA LSDQIGKPVR
     LVVSVDTSLE RTVAPDEAAS PATVTPLQPR DLPREDRDGH DDRDDREARD RRREQHDRER
     DRDERRDRQD DSPLHRHRDM STKASSSLTT GIPDSPLNPR YSFETFVIGS SNRFAHAAAV
     AVAEAPGKAY NPLMVYGDSG LGKTHLLHAI GHYVRNLWTG AKIRYVSSEA FTNDVINAIK
     DANTAALQRR YRDVDVLLVD DIQFLEGKQQ TQEEFFHTFN TLHNANKQIV ISSDRSPKRL
     TQLEDRLRNR FEWGLLTDVQ PPDLETRIAI LRKKAAADRL SAPADVLEFI ASRIQTNIRE
     LEGALIRVTA FASINQQEVD MTLAEIVLRD LIPEGGEPEV TAGLIIAQTA SYFGFSIEDL
     TGPSRTRALV TARQISMYLC RELTELSLPK IGQQFGGRDH TTVMNADRRI RKDLAERRNV
     FHQVTELTTR IKQQAKQA
//
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