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Database: UniProt
Entry: A0A101IHS8_9BACT
LinkDB: A0A101IHS8_9BACT
Original site: A0A101IHS8_9BACT 
ID   A0A101IHS8_9BACT        Unreviewed;       445 AA.
AC   A0A101IHS8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   20-JUN-2018, entry version 17.
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   ORFNames=XE05_0031 {ECO:0000313|EMBL:KUK95423.1};
OS   Thermotogales bacterium 46_20.
OC   Bacteria; Thermotogae; Thermotogales.
OX   NCBI_TaxID=1635293 {ECO:0000313|EMBL:KUK95423.1, ECO:0000313|Proteomes:UP000054930};
RN   [1] {ECO:0000313|EMBL:KUK95423.1, ECO:0000313|Proteomes:UP000054930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=46_20 {ECO:0000313|EMBL:KUK95423.1};
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}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00747961}.
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:KUK95423.1}.
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DR   EMBL; LGGZ01000001; KUK95423.1; -; Genomic_DNA.
DR   PATRIC; fig|1635293.3.peg.535; -.
DR   Proteomes; UP000054930; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054930};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00747973};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00748008};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054930}.
FT   DOMAIN      133    325       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      348    416       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     141    148       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   445 AA;  51330 MW;  5A3DBCA7F2047837 CRC64;
     MSRKILDVLR DSVPKKTWNN WFSSLEVKKI DHDRVELTVD NLFIKDWLQT RFSKEITNAI
     RAATGRELPF TIQDKNISSQ SKSESVSQES LVRKRPLQLS NLSEECTFEN FQFGIENRFL
     VEAGREISLN PGAYNPLFIY GGVGLGKTHI MQAIARRAMD IHPEKRIIYI TSEQFLNEMV
     VAIKKNEVHR FREEYRRKAD ALLIDDIQFL VGKKGVQNEF FHTFNHLHDA GKQLVICSDR
     SPEELEDFHE RYVSRFQMGL AIRISEPSEE TRFLIAKGLA KRENVEISDE VAWFLARNVD
     ANIRRLRGAI IKMIVQAKIY EQDYDLSLAT EVLRSMNIGT FSGQTKSPVE LLFSCIKELT
     GFEKEELLAS SRDAERVRAR YLFIYGMKNT LGRSINEIAS TIRRKHSTVI HALKKIEKAL
     EQKDDTITEP VNRLFTSMSS KSQAS
//
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