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Database: UniProt
Entry: G9PRN8_9BACT
LinkDB: G9PRN8_9BACT
Original site: G9PRN8_9BACT 
ID   G9PRN8_9BACT            Unreviewed;       444 AA.
AC   G9PRN8;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   05-JUL-2017, entry version 41.
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=HMPREF1006_02810 {ECO:0000313|EMBL:EHL71483.1};
OS   Synergistes sp. 3_1_syn1.
OC   Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae;
OC   Synergistes.
OX   NCBI_TaxID=457415 {ECO:0000313|EMBL:EHL71483.1, ECO:0000313|Proteomes:UP000003380};
RN   [1] {ECO:0000313|EMBL:EHL71483.1, ECO:0000313|Proteomes:UP000003380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3_1_syn1 {ECO:0000313|EMBL:EHL71483.1,
RC   ECO:0000313|Proteomes:UP000003380};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.,
RA   Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L.,
RA   Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Synergistes sp. 3_1_syn1.";
RL   Submitted (SEP-2011) 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:SAAS00731907}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00756131}.
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:EHL71483.1}.
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DR   EMBL; ACUH01000001; EHL71483.1; -; Genomic_DNA.
DR   RefSeq; WP_008708497.1; NZ_JH414690.1.
DR   EnsemblBacteria; EHL71483; EHL71483; HMPREF1006_02810.
DR   PATRIC; fig|457415.3.peg.44; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000003380; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
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:SF12; PTHR30050:SF12; 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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000003380};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003380}.
FT   DOMAIN      141    269       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      354    423       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     149    156       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   444 AA;  50470 MW;  7306376F00AFF928 CRC64;
     MDLDIIWKEY YKYCMEKLGT EDKTAEIYLQ TCMPLSLDDG VLTLDVATQF AMDQIKSRYL
     ARMRELLIET SFGTDVRLRV SSDQPEDTRV QEPQPKAQPP KPASGRNGLN PNYVFSTFVV
     GKSNRLPHAA SLAVAESPGN TYNPFFIWGK VGLGKTHLMH AIGHHIEATN NNTKILYVSA
     EKFTNDLITA IRNNTNQEFR ARYRELDVLM IDDVQFIAGK EQTQEEFFWT FNTLHDAKKQ
     IIISADRPPK DIEGIADRLV SRFEWGLVTD IQPPDLETRV AILQKKAEMK KYMNIPEDVI
     MFIAQNIPSN IRELEGSLNR IVACSDLNHE PINIENASVW LKDLIKEHPV GTVSIGLIQQ
     MTAEAFGFSV EELLSKKRTA DLALARQAAM YVARNKTNEA LIQIAYAFNK KDHTVVIHAC
     RKIAELIKTD LRIRSFVDNI VNKL
//
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