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Database: UniProt
Entry: A0A136MF06_9BACT
LinkDB: A0A136MF06_9BACT
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ID   A0A136MF06_9BACT        Unreviewed;       503 AA.
AC   A0A136MF06;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   05-JUL-2017, entry version 10.
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:KXK32492.1};
GN   ORFNames=UZ06_CHB003002122 {ECO:0000313|EMBL:KXK32492.1};
OS   Chlorobi bacterium OLB6.
OC   Bacteria; Chlorobi.
OX   NCBI_TaxID=1617413 {ECO:0000313|EMBL:KXK32492.1, ECO:0000313|Proteomes:UP000070423};
RN   [1] {ECO:0000313|EMBL:KXK32492.1, ECO:0000313|Proteomes:UP000070423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB6 {ECO:0000313|EMBL:KXK32492.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Dutilh B.E., Jetten M.S.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (OCT-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, ECO:0000256|SAAS:SAAS00724167}.
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:KXK32492.1}.
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DR   EMBL; LLZP01000053; KXK32492.1; -; Genomic_DNA.
DR   PATRIC; fig|1617413.3.peg.2230; -.
DR   Proteomes; UP000070423; 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; 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: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.
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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000070423};
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:UP000070423}.
FT   DOMAIN      199    327       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      411    480       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     207    214       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   503 AA;  56389 MW;  F16C91D97BA34130 CRC64;
     MSKHDELNLF STTQVAAGTP TAATASERSA RSGGTSDAET LWARCLEIIR DNVSEQVFST
     WFEQIRPSSW DGTTLTIELP SNFFYEWLEE HYAQLIKKTT QKILGARSKV RYRVVVEKDS
     AEPSNAVYLP AGHGMQQPAL PFHAPKSSSP SAPQAQGPAV HYLSYFNPRH TFENFIRGES
     NQLAISAAMA VADNPGGTSY NPLVIYGPTG LGKTHLVQAI GNRVLQRNRS AKVLYTNSEK
     FTMEYINAIQ TNKVPDFTNF YRGVDVLIVD DIQFLGGKEK TQDQFFHTFN ALLSIGKQVV
     LTSDKQPKDL ADVDERLISR FVWGLMADIQ PPDFETRMAI LQQKALEEGV DLPGDILEFV
     ARNVSSSVRE IEGCLISILA KVTLDNRELS LELAKDVVRN VTSSPSARQL TIEDIKQEVS
     VYYNQPIELL SAKTRKHEVV LPRQMCMYLA KHLTQMSLKS IGMHFGGRDH TTVLHSCQQI
     SNYIDTDRKV RQDVEFLKKA LRS
//
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