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Database: UniProt
Entry: A0A136KG17_9BACT
LinkDB: A0A136KG17_9BACT
Original site: A0A136KG17_9BACT 
ID   A0A136KG17_9BACT        Unreviewed;       461 AA.
AC   A0A136KG17;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   05-JUL-2017, entry version 11.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:KXK08253.1};
GN   ORFNames=UZ20_WS6002000781 {ECO:0000313|EMBL:KXK08253.1};
OS   candidate division WS6 bacterium OLB21.
OC   Bacteria; Candidatus Dojkabacteria.
OX   NCBI_TaxID=1617427 {ECO:0000313|EMBL:KXK08253.1, ECO:0000313|Proteomes:UP000070449};
RN   [1] {ECO:0000313|EMBL:KXK08253.1, ECO:0000313|Proteomes:UP000070449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB21 {ECO:0000313|EMBL:KXK08253.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Improved understanding of the partial-nitritation anammox process
RT   through 23 genomes representing the majority of the microbial
RT   community.";
RL   Submitted (FEB-2015) 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}.
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:KXK08253.1}.
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DR   EMBL; JYPD01000025; KXK08253.1; -; Genomic_DNA.
DR   PATRIC; fig|1617427.3.peg.812; -.
DR   Proteomes; UP000070449; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
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; 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.
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:UP000070449};
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:UP000070449}.
FT   DOMAIN      155    286       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      366    435       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     163    170       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   461 AA;  52168 MW;  A1595C0AC709DEDE CRC64;
     MDLQEIWKIT LAQIEIKLDS PAQFKTWFKD TKLREIRGSH AIIGVKNSYT SDWLSKKHSK
     LIKDTLSYVH GSDLTVAFEI DSSLANKPNP VITPEELTAD TPIFGLHQGQ DSSTDQILKN
     SGLNSNYSFA NYIVGPSNKL GHAAALAVAK KPGESYNPLF VYGKTGLGKT HLAHAVGRAI
     LESDPYKKVL YVSSEGFLND MVKAIRSGKN IQFRQKYRTL DLLIIDDIQF IYKWKETQNE
     FFNTFNVLYN DKKQIILISD RSPDEIQGIE DRLRSRFQGG MTVDIEKPDF EMRLALVESK
     SKTMGISLPI HINEFIAKNI TENVRELEGA IQKVSLYSSM VQEDLSLEEV AKILGKDTSS
     KREKTKVPAI LKCIAKEFNT TVKDLKGPRR TADVAFARQV CMYLLREDYG YKLEQVAAYI
     NRKDHTTVLH AVDKIKSKLM IDEGFKNQID SLRETISGND D
//
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