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Database: UniProt
Entry: A0A136KQT3_9BACT
LinkDB: A0A136KQT3_9BACT
Original site: A0A136KQT3_9BACT 
ID   A0A136KQT3_9BACT        Unreviewed;       380 AA.
AC   A0A136KQT3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   05-JUL-2017, entry version 9.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000313|EMBL:KXK11816.1};
GN   ORFNames=UZ22_OP11002000263 {ECO:0000313|EMBL:KXK11816.1};
OS   Microgenomates bacterium OLB23.
OC   Bacteria; Candidatus Microgenomates.
OX   NCBI_TaxID=1617429 {ECO:0000313|EMBL:KXK11816.1, ECO:0000313|Proteomes:UP000070280};
RN   [1] {ECO:0000313|EMBL:KXK11816.1, ECO:0000313|Proteomes:UP000070280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB23 {ECO:0000313|EMBL:KXK11816.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-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|RuleBase:RU000577}.
CC   -!- SIMILARITY: Belongs to the DnaA family.
CC       {ECO:0000256|RuleBase:RU004227, 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:KXK11816.1}.
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DR   EMBL; LMZU01000006; KXK11816.1; -; Genomic_DNA.
DR   PATRIC; fig|1617429.3.peg.289; -.
DR   Proteomes; UP000070280; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:InterPro.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR001957; Chromosome_initiator_DnaA.
DR   InterPro; IPR020591; Chromosome_initiator_DnaA-like.
DR   InterPro; IPR013317; DnaA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR30050:SF12; PTHR30050:SF12; 1.
DR   Pfam; PF00308; Bac_DnaA; 1.
DR   PRINTS; PR00051; DNAA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU000577};
KW   Complete proteome {ECO:0000313|Proteomes:UP000070280};
KW   DNA replication {ECO:0000256|RuleBase:RU004227};
KW   DNA-binding {ECO:0000256|RuleBase:RU000577};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000577};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070280}.
FT   DOMAIN      105    263       AAA. {ECO:0000259|SMART:SM00382}.
SQ   SEQUENCE   380 AA;  43289 MW;  55664BD8F4066CD5 CRC64;
     MFLDGRKKII EKHLSDFLQK EVQLEILIKP PKKKKGKKEE KEQTPLAEEG PSTGLPLIDY
     KDSLEGVLKK AHIQDRYTFE NFAVSATNHV AHAAAQAVAE NPARIYNPLF IYGDVGVGKT
     HLSHAIANHI LQKNIQQKVL YCTSEQFTND LVESIKVKNT RELRKKYREL DLLIIDDVQF
     IAGKSYVQEE FYHTFNAIVQ GGGQSWSLIS DRPPKEIKEL EDRLRSRFSG GLILDIQKPD
     FELRTAILLI KAEERHIDID IDAAKEIAEK VTDSRELEGT LLRLLSVSLM ESQSNKITME
     TTQGELGMQA ARIAQKVSPH DVIKNLCLYY QIKPSIIKKP QLAHRLFQTY AKLLCMCFVE
     RLVLTSLRLP LCSTEKTIQP
//
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