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Database: UniProt
Entry: D7N2G6_9NEIS
LinkDB: D7N2G6_9NEIS
Original site: D7N2G6_9NEIS 
ID   D7N2G6_9NEIS            Unreviewed;       504 AA.
AC   D7N2G6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   05-JUL-2017, entry version 44.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:EFI23778.1};
GN   ORFNames=HMPREF9016_02174 {ECO:0000313|EMBL:EFI23778.1};
OS   Neisseria sp. oral taxon 014 str. F0314.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=641149 {ECO:0000313|EMBL:EFI23778.1, ECO:0000313|Proteomes:UP000002768};
RN   [1] {ECO:0000313|EMBL:EFI23778.1, ECO:0000313|Proteomes:UP000002768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0314 {ECO:0000313|EMBL:EFI23778.1,
RC   ECO:0000313|Proteomes:UP000002768};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA   Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T.,
RA   White J., Yandava C., Izard J., Baranova O.V., Blanton J.M.,
RA   Tanner A.C., Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Neisseria sp. oral taxon 014 strain F0314.";
RL   Submitted (FEB-2010) 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:SAAS00724167}.
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}.
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DR   EMBL; GL349412; EFI23778.1; -; Genomic_DNA.
DR   RefSeq; WP_009174414.1; NZ_GL349412.1.
DR   STRING; 641149.HMPREF9016_02174; -.
DR   EnsemblBacteria; EFI23778; EFI23778; HMPREF9016_02174.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000002768; 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; IPR024633; DnaA_N_dom.
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   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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002768};
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}.
FT   DOMAIN      201    331       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      412    481       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     209    216       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   504 AA;  56695 MW;  5BDF0DFE6B16CDFA CRC64;
     MTLAEFWPLC LRKLHDSLPA QQFQTWIAPL TVGEENGTWV VYGKNQFACN MLQNRFAADI
     EAVRAELAPQ QAAFLFKTGT GRSYPMASDA SGKSLEERPS ENTPAHPHTT PALSNKTAAD
     ILAERMKNLP HGNRRTEPEP APAAANPTAK TRLDEQRGAA ETRYSQTNLS SDYTFETLVE
     GKGNRIAAAA AQSIAENPGQ SYNPFFLYGS TGLGKTHLVQ AIGNELLKNR PDAKVRYMHS
     DDYIRSFMSA VRTNSYDVFK QQYKQYDLLI IDDIQFIKGK DRTMEEFFYL YNHFHNEKKQ
     LILTCDVLPA KIEDMDDRLK SRFSWGLTLE LEPPELEMRV AILQKKAESS GISLTDEAAF
     FIANLIRSNV RELEGAFNRV SASSRFMNKP IDIDLARDAL QDIIAVKHKV ITADIIIDAT
     AKYYRIKISD ILGKKRTRNI ARPRQVAMSL TKELTNLSLP SIGDAFGGRD HTTVMHGVKA
     VAKLREDDPE LAQDYEKLLI MIQN
//
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