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Database: UniProt
Entry: A0A101HVR6_9BACT
LinkDB: A0A101HVR6_9BACT
Original site: A0A101HVR6_9BACT 
ID   A0A101HVR6_9BACT        Unreviewed;       449 AA.
AC   A0A101HVR6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-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, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=XD98_0273 {ECO:0000313|EMBL:KUK83699.1};
OS   Microgenomates bacterium 39_6.
OC   Bacteria; Candidatus Microgenomates.
OX   NCBI_TaxID=1641391 {ECO:0000313|EMBL:KUK83699.1, ECO:0000313|Proteomes:UP000053541};
RN   [1] {ECO:0000313|EMBL:KUK83699.1, ECO:0000313|Proteomes:UP000053541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=39_6 {ECO:0000313|EMBL:KUK83699.1};
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-resolved metagenomic analysis reveals roles for candidate
RT   phyla and other microbial community members in biogeochemical
RT   transformations in oil reservoirs.";
RL   MBio 7:e01669-15(2015).
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:KUK83699.1}.
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DR   EMBL; LGGT01000031; KUK83699.1; -; Genomic_DNA.
DR   PATRIC; fig|1641391.3.peg.249; -.
DR   Proteomes; UP000053541; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053541};
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:UP000053541}.
FT   DOMAIN      146    280       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      357    426       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     154    161       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      426    449       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   449 AA;  51223 MW;  471E9D1E2DBAA7C4 CRC64;
     MDLKSLWQDV QEELKISVSQ TTYQGMLAQT TLLDLKKNIA TIGCPNPYLR DLIENRYYSL
     IKEVLDRQTK EKNSLVFAID QNQTNSKKIK NLGPLFKKRP DQKPNNQVNP DFGLLPNYNF
     ETFVVGSANN FAHAAAQAIV KNPGQTYNPF FVWGGVGVGK THLTHAIGNA IAKKNKNFKI
     LYVSAETFTN ELVEALQKKT ITKFKDKYRK CDCLLVDDIQ FIAGKEYSQE EFFHTFNALY
     LSGRQVVLTS DRKPEEIPKV EDRLISRFMG GLTVDIQPPD YEMRLAILKQ KAQEKNFSLS
     EEVAAFLAET IESNIRELEG ALLRLIIKTQ SNDSQVDLEF AQNLFGSLKK KKAKRVTPRT
     VLSRTAKHFS FKTKELCGKS RKSELVTARH IAIYLLRKDL DLPLMKIGDL VGGRDHTSIM
     YAIDKIEREY SNNQSLRSNI NQIRNNLQS
//
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