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Database: UniProt
Entry: I8UH41_9BACI
LinkDB: I8UH41_9BACI
Original site: I8UH41_9BACI 
ID   I8UH41_9BACI            Unreviewed;       451 AA.
AC   I8UH41;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   25-OCT-2017, entry version 37.
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:EIT86128.1};
GN   ORFNames=A374_07401 {ECO:0000313|EMBL:EIT86128.1};
OS   Fictibacillus macauensis ZFHKF-1.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX   NCBI_TaxID=1196324 {ECO:0000313|EMBL:EIT86128.1, ECO:0000313|Proteomes:UP000004080};
RN   [1] {ECO:0000313|EMBL:EIT86128.1, ECO:0000313|Proteomes:UP000004080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZFHKF-1 {ECO:0000313|EMBL:EIT86128.1,
RC   ECO:0000313|Proteomes:UP000004080};
RX   PubMed=22887677; DOI=10.1128/JB.01049-12;
RA   Cai L., Zhang T.;
RT   "Genome of Bacillus macauensis ZFHKF-1, a Long-Chain-Forming
RT   Bacterium.";
RL   J. Bacteriol. 194:4780-4780(2012).
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: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:EIT86128.1}.
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DR   EMBL; AKKV01000023; EIT86128.1; -; Genomic_DNA.
DR   RefSeq; WP_007201577.1; NZ_AKKV01000023.1.
DR   EnsemblBacteria; EIT86128; EIT86128; A374_07401.
DR   PATRIC; fig|1196324.3.peg.1515; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000004080; 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:SF2; PTHR30050:SF2; 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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000004080};
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:UP000004080}.
FT   DOMAIN      147    275       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      359    428       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     155    162       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   451 AA;  51196 MW;  09C74B6E0F885FB3 CRC64;
     MENINDLWNK ALAAIEKKVS KPSFETWLKS TVAHALQKDT LIITAPNEFA RDWLESHYSP
     LISETLLDVT GAALDVKFII PQHQIEEEVD LDKVLKASQK ANSEQQEEVI SQSMLNPKYT
     FDRFVIGSGN RFAHAASLAV AEAPAKAYNP LFIYGGVGLG KTHLMHAIGH YVIDHKPNAK
     VVYLSSEKFT NEFINSIRDN KTVEFRNKFR SVDVLLIDDI QFLAGKEQTQ EEFFHTFNAL
     HEESKQIVIS SDRPPKEIPT LEDRLRSRFE WGLITDITPP DLETRIAILR KKAKAEGLDI
     PNEVMLYIAN QIDTNIRELE GALIRVVAYS SLINQDMNAD LAAEALKDII PSSKPRTITI
     HHIQEVVGRH YNVKLEDFTA KKRTKSVAFP RQIAMYLARE LTDNSLPKIG EEFGGRDHTT
     VLHAHEKISN LMISDQQLQK NMKEIHDQLK S
//
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