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Database: UniProt
Entry: A0A0C2HKV2_9DELT
LinkDB: A0A0C2HKV2_9DELT
Original site: A0A0C2HKV2_9DELT 
ID   A0A0C2HKV2_9DELT        Unreviewed;       452 AA.
AC   A0A0C2HKV2;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   16-JAN-2019, entry version 30.
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=GFER_03045 {ECO:0000313|EMBL:KIH77661.1};
OS   Geoalkalibacter ferrihydriticus DSM 17813.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geoalkalibacter.
OX   NCBI_TaxID=1121915 {ECO:0000313|EMBL:KIH77661.1, ECO:0000313|Proteomes:UP000035068};
RN   [1] {ECO:0000313|EMBL:KIH77661.1, ECO:0000313|Proteomes:UP000035068}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17813 {ECO:0000313|EMBL:KIH77661.1,
RC   ECO:0000313|Proteomes:UP000035068};
RA   Badalamenti J.P., Torres C.I., Krajmalnik-Brown R., Bond D.R.;
RT   "Genomes of Geoalkalibacter ferrihydriticus and Geoalkalibacter
RT   subterraneus, two haloalkaliphilic metal-reducing members of the
RT   Geobacteraceae.";
RL   Submitted (DEC-2014) 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:KIH77661.1}.
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DR   EMBL; JWJD01000001; KIH77661.1; -; Genomic_DNA.
DR   RefSeq; WP_040095933.1; NZ_JWJD01000001.1.
DR   EnsemblBacteria; KIH77661; KIH77661; GFER_03045.
DR   OrthoDB; 219876at2; -.
DR   Proteomes; UP000035068; 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   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   Complete proteome {ECO:0000313|Proteomes:UP000035068};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035068}.
FT   DOMAIN      149    277       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      360    429       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     157    164       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   452 AA;  51613 MW;  A1C3EFBD13DE5261 CRC64;
     MDRLWQETLE HLKEIISPQL FSTWIKPIHF IRVEKSTVFL QVPNRFFLDW IRDNYASRIE
     QALSTMGAVD YHVVLEVGKP ENAIGTPAES DANQNFSAPV EKEIFPQKKP EFFPSNLNPR
     YVFNDFVSGS SNQFAHAAAM AVANNPATTY NPLFIYGGVG LGKTHLVNAI GNAILKKNPD
     MRVCYYASEK FMNELINSLR YARMDEFRNK FRSMDVLLID DVQFIAGKER TQEEFFHTFN
     ALYEAHKQIV VTSDKFPKDI PGLEERLRSR FEWGLIADIQ APDVETKQAI LKMKAEKNAI
     PLPEDVAYFL SNSVTSNVRE LEGFLIRLGA YASLTSTSIT LEMAREVLKD ILVEKNKELT
     VEEIQKTVAA HFNIKMADLK SPKRLKALVL PRQIAMYLAR NLTSLSFPEI GERFGGKDHS
     TIIHAIKKID RCQEDDFQLR AVITTLKNNL TR
//
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