GenomeNet

Database: UniProt
Entry: A0A0S7YPH0_9BACT
LinkDB: A0A0S7YPH0_9BACT
Original site: A0A0S7YPH0_9BACT 
ID   A0A0S7YPH0_9BACT        Unreviewed;       443 AA.
AC   A0A0S7YPH0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   25-OCT-2017, entry version 13.
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=AMS14_01865 {ECO:0000313|EMBL:KPJ76606.1};
OS   Planctomycetes bacterium DG_20.
OC   Bacteria; Planctomycetes.
OX   NCBI_TaxID=1703413 {ECO:0000313|EMBL:KPJ76606.1, ECO:0000313|Proteomes:UP000052133};
RN   [1] {ECO:0000313|EMBL:KPJ76606.1, ECO:0000313|Proteomes:UP000052133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG_20 {ECO:0000313|EMBL:KPJ76606.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur
RT   cycling among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:SAAS00747914}.
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:KPJ76606.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; LIZP01000027; KPJ76606.1; -; Genomic_DNA.
DR   PATRIC; fig|1703413.3.peg.2188; -.
DR   Proteomes; UP000052133; 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; 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.
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:UP000052133};
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:UP000052133}.
FT   DOMAIN      139    270       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      350    419       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     147    154       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   443 AA;  49762 MW;  BFC4D4AD59D2DD91 CRC64;
     MAPAEPNLWQ QALDHLSGQF SDLPIPLWLT QAHLDELDAS HLAVTLPAAA READVTAALR
     SALHRALERA VGRQLDVEFR SGGVADVQPP RPAPSPEGGL RGDHPPLNPL YVFENFVTGP
     CNRMAHASAL AVSDLPGRAY NPLFIHASVG LGKSHLMQAI CHKLLQTRPG VAMMYLSCED
     FVNQFIAAIE RGQVAEFRYK FRYLDVLIID DVHFLADKDR TQEEFFHTFN ALYQAQKQVV
     LSSDSPPHEI PRIEERLVSR FKWGLVVRID RPSYETRVAI VRKKARLRNQ ELPEDVVQYI
     ATVVDTNNRE LEGAVVRVLG HASLDDRKID IDLTKETLRD MVAAPSRAIT IAAIAEAVLQ
     RFNVRLSDLQ SKRRAQSVAL PRQICMYLAR RLTNRSLEEV GAFFGGRDHT TVLHAERKIG
     RMVKRDPGFR GLVEAIETHV LRQ
//
DBGET integrated database retrieval system