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Database: UniProt
Entry: A0A1R0IK93_SULTH
LinkDB: A0A1R0IK93_SULTH
Original site: A0A1R0IK93_SULTH 
ID   A0A1R0IK93_SULTH        Unreviewed;       463 AA.
AC   A0A1R0IK93;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   16-JAN-2019, entry version 14.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=C7B47_06625 {ECO:0000313|EMBL:PSR27946.1};
OS   Sulfobacillus thermosulfidooxidans.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Clostridiales Family XVII. Incertae Sedis; Sulfobacillus.
OX   NCBI_TaxID=28034 {ECO:0000313|EMBL:PSR27946.1};
RN   [1] {ECO:0000313|EMBL:PSR27946.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AMDSBA5 {ECO:0000313|EMBL:PSR27946.1};
RX   PubMed=25511286; DOI=.1186/1471-2164-15-1107;
RA   Justice N.B., Norman A., Brown C.T., Singh A., Thomas B.C.,
RA   Banfield J.F.;
RT   "Comparison of environmental and isolate Sulfobacillus genomes reveals
RT   diverse carbon, sulfur, nitrogen, and hydrogen metabolisms.";
RL   BMC Genomics 15:1107-1107(2014).
RN   [2] {ECO:0000313|EMBL:PSR27946.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AMDSBA5 {ECO:0000313|EMBL:PSR27946.1};
RA   Keele B.F.;
RL   Submitted (MAR-2018) 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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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:PSR27946.1}.
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DR   EMBL; PXYX01000009; PSR27946.1; -; Genomic_DNA.
DR   RefSeq; WP_020375201.1; NZ_MDZF01000019.1.
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   Gene3D; 3.30.300.180; -; 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; IPR038454; DnaA_N_sf.
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:SAAS00756129};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117}.
FT   NP_BIND     166    173       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   463 AA;  52403 MW;  2B88514FF70D97B3 CRC64;
     MLEVGLESLW ADTVARLESE LSTPSIETWV RQVFPLSLED GVLELAVPSD FVRQIIASRY
     TGLLRDVLAK SAGRPIDVHL ILTPKSSETV YNEKPVPVPI SVTQESRPPV NKEPSETTES
     EFHTRLNPKY VFEAFVVGVS NRFAHAACQA VAEMPARAYN PLFLYGGVGL GKTHLMHAIG
     HHVLAGSPKA RVLYVSSENF TNEMINAIRD DKMVRFRQRY RNIDVLLIDD IQFVAGKERT
     QEEFFHTFEA LHGAHKQIVI SSDRPPKDIP TLEERLRSRF EWGLITDIQP PDLETRIAIL
     AKKAQLEDLS VPDSVLQFIA TRIDTNIREL EGALIRVMAY GSITRQPLTA ELAMEALKDV
     IPNSRPKPIT IRLIQEEVAK HFDLRVEDLK AKKRTRTVAF PRQVAMYMAR QLTDSSLPRI
     GEEFGGRDHT TVIHACEKIE QERHTDTQLA QLLEALTKRI KSR
//
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