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Database: UniProt
Entry: A0A0C2VW84_9PROT
LinkDB: A0A0C2VW84_9PROT
Original site: A0A0C2VW84_9PROT 
ID   A0A0C2VW84_9PROT        Unreviewed;       441 AA.
AC   A0A0C2VW84;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   25-OCT-2017, entry version 22.
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   ORFNames=KU29_01005 {ECO:0000313|EMBL:KIM09867.1};
OS   Sulfurovum sp. FS06-10.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Sulfurovum.
OX   NCBI_TaxID=1539064 {ECO:0000313|EMBL:KIM09867.1, ECO:0000313|Proteomes:UP000031944};
RN   [1] {ECO:0000313|EMBL:KIM09867.1, ECO:0000313|Proteomes:UP000031944}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=25620962; DOI=10.3389/fmicb.2014.00756;
RA   Hamilton T.L., Jones D.S., Schaperdoth I., Macalady J.L.;
RT   "Metagenomic insights into S(0) precipitation in a terrestrial
RT   subsurface lithoautotrophic ecosystem.";
RL   Front. Microbiol. 5:756-756(2014).
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:KIM09867.1}.
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DR   EMBL; JQIR01000001; KIM09867.1; -; Genomic_DNA.
DR   EnsemblBacteria; KIM09867; KIM09867; KU29_01005.
DR   Proteomes; UP000031944; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031944};
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:UP000031944}.
FT   DOMAIN      137    263       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      346    415       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     145    152       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      415    441       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   441 AA;  50478 MW;  6438BCB4A179485C CRC64;
     MLADTVLSLL KEEISSLEYD RYVKQLKFHE KASNSEQMVF IAPNVLIANW VKLKYSEKLS
     HLFELKTGKK PEIKIVLKEH IKTNKIKTIP LEMVDVIKLT KNTILNPSYT FNSFVVGSSN
     QYAYTAAKSV AEKPGIIYNP VFIYGPTGLG KTHLIHAIGN YVQNKGKSVI YATIEQFMND
     FTYNLRNQSM DRFRDKYRNC DVLLIDDAQF LSNKIQTQEE FFHTFNELHS AGKQIVLTSD
     KPPKMINGLE DRLKSRFEWG LIADIGLPEL ETKIAIIEKK CELDGINLGS DIVNYIAANM
     GDNIREIESA IINLNAYASL MRQEITLDFA KNVMREQIKE RRENITLEDI IATISKDLNI
     KPSEIKSTKR SKNIVEARRI GIYLARTLTP NSMPSLASYF GMKDHTAVSH NIKKINELIM
     TNESFKLRVE ELKNKILTKQ L
//
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