GenomeNet

Database: UniProt
Entry: A0A1I2HP08_9BACT
LinkDB: A0A1I2HP08_9BACT
Original site: A0A1I2HP08_9BACT 
ID   A0A1I2HP08_9BACT        Unreviewed;       488 AA.
AC   A0A1I2HP08;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   16-JAN-2019, entry version 10.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=SAMN04488541_102538 {ECO:0000313|EMBL:SFF31539.1};
OS   Thermoflexibacter ruber.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Thermoflexibacter.
OX   NCBI_TaxID=1003 {ECO:0000313|EMBL:SFF31539.1, ECO:0000313|Proteomes:UP000199513};
RN   [1] {ECO:0000313|EMBL:SFF31539.1, ECO:0000313|Proteomes:UP000199513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GEY, DSM 9560 {ECO:0000313|Proteomes:UP000199513};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC       ECO:0000256|SAAS:SAAS00555179}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; FONY01000025; SFF31539.1; -; Genomic_DNA.
DR   Proteomes; UP000199513; 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; IPR018312; Chromosome_initiator_DnaA_CS.
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.
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:SAAS00756129};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000199513};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199513}.
FT   DOMAIN      179    309       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      393    462       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     187    194       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      371    391       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   488 AA;  55518 MW;  D12F5521DA7FA776 CRC64;
     MSMPDKMLTN ITTKDCELVW KNCLKVIRAS VGEQSFKTWF EPIRPVKLHH TVLTIQVPSQ
     FFYEWLEEHY VNVLKKAIYS ELGAEGKLEY SIIIDKGNEQ HQPFTINISN PKNVKPVDHS
     PLPTQKQFFS PFDMRTVPPH HAHSNLSNKY SFENFIEGEC NRLAYSASFS VAHNPGATAF
     NPLVIHGGVG LGKTHLLHAI GNEVKALFPE KFVLYVPSDL FITQFVDALK NQAVQEFTNY
     YMQVEVLLVD DIQFLAGKEK TQENFFHIFN YLHQSGKQIV MTCDTAPKDL KGLHDRLLSR
     FKWGLVADVQ VPDYTTRLSI VKAKMQTEGI KIPNEVVEYV AKNVDTNVRE LQGVLISLVA
     KASLMRQEID IDLTEKTLNQ IIQNVKQIEV DLNIELIQKA VAEHFNVSLD DLLSGTRKKE
     VANARQIAMF ICQNYTNMSL KAIGEYFGGR DHSTVSHASR TVTERLENDP LYKNIIEALK
     AKLNLRGK
//
DBGET integrated database retrieval system