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Database: UniProt
Entry: U7UH30_9FIRM
LinkDB: U7UH30_9FIRM
Original site: U7UH30_9FIRM 
ID   U7UH30_9FIRM            Unreviewed;       487 AA.
AC   U7UH30;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-SEP-2017, entry version 31.
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:ERT58737.1};
GN   ORFNames=HMPREF1250_1869 {ECO:0000313|EMBL:ERT58737.1};
OS   Megasphaera sp. BV3C16-1.
OC   Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=1111454 {ECO:0000313|EMBL:ERT58737.1, ECO:0000313|Proteomes:UP000017090};
RN   [1] {ECO:0000313|EMBL:ERT58737.1, ECO:0000313|Proteomes:UP000017090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BV3C16-1 {ECO:0000313|EMBL:ERT58737.1,
RC   ECO:0000313|Proteomes:UP000017090};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M.,
RA   Haft D.H., Methe B., Sutton G., Nelson K.E.;
RL   Submitted (SEP-2013) 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}.
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:ERT58737.1}.
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DR   EMBL; AWXA01000041; ERT58737.1; -; Genomic_DNA.
DR   RefSeq; WP_023054036.1; NZ_AWXA01000041.1.
DR   EnsemblBacteria; ERT58737; ERT58737; HMPREF1250_1869.
DR   PATRIC; fig|1111454.3.peg.1537; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000017090; 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; 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:UP000017090};
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:UP000017090}.
FT   DOMAIN      179    310       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      392    461       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     187    194       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   487 AA;  56208 MW;  67FBFAE389560C39 CRC64;
     METTDLIEIW EGILRELQKK VDPKIYTTWF ETSIIPYMYQ NDTLILDTTN KFICLYITRK
     YGQLLKETAT LVIGSETNVE LINSEDKTII PEEPVAETIH HVKPQQQQPA DTEPTVQEEL
     TQISSVPSAT TEQRNTDTIK PTGYTELNDM YTFDNFIVGN SNRIAYSAAL SIAEAPAKKY
     NPFFIYGGSG LGKTHLMQAI GHSLLEKFPT LRLHCITSED FTNDMIHSLR DKNPESFRQK
     YRNIDVLLVD DIQFLEDKER TQEEFFHTFN TLFRDRKQMV FTSDRPPQDI KKLEDRLRSR
     FQGGMVVNID PPDLETRMAI LLSLAQKEHI AVDKKAIDYI ASYMSTNVRE LEGAFFRAQM
     QASAENSPIT LEITQKALKE LVSVNNDKKY ITIDEITATV CRFYKVKYED LMSKKKTKNI
     ALPRQIAMYL CRELTENTYP HIGTAFNGRD HTTVMHACTK IMKTMETDEH FRAMIEELKN
     KIKNVNA
//
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