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Database: UniProt
Entry: A0A292YBD5_9PROT
LinkDB: A0A292YBD5_9PROT
Original site: A0A292YBD5_9PROT 
ID   A0A292YBD5_9PROT        Unreviewed;       436 AA.
AC   A0A292YBD5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   13-FEB-2019, entry version 10.
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=LNAT_P0045 {ECO:0000313|EMBL:GAX86750.1};
OS   Lebetimonas natsushimae.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales;
OC   Nautiliaceae; Lebetimonas.
OX   NCBI_TaxID=1936991 {ECO:0000313|EMBL:GAX86750.1, ECO:0000313|Proteomes:UP000217944};
RN   [1] {ECO:0000313|EMBL:GAX86750.1, ECO:0000313|Proteomes:UP000217944}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS1857 {ECO:0000313|EMBL:GAX86750.1,
RC   ECO:0000313|Proteomes:UP000217944};
RX   PubMed=28690052; DOI=.1016/j.syapm.2017.06.002;
RA   Nagata R., Takaki Y., Tame A., Nunoura T., Muto H., Mino S.,
RA   Sawayama S., Takai K., Nakagawa S.;
RT   "Lebetimonas natsushimae sp. nov., a novel strictly anaerobic,
RT   moderately thermophilic chemoautotroph isolated from a deep-sea
RT   hydrothermal vent polychaete nest in the Mid-Okinawa Trough.";
RL   Syst. Appl. Microbiol. 40:352-356(2017).
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: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   -!- 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:GAX86750.1}.
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DR   EMBL; BDME01000001; GAX86750.1; -; Genomic_DNA.
DR   Proteomes; UP000217944; 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:SAAS00756129};
KW   Complete proteome {ECO:0000313|Proteomes:UP000217944};
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}.
FT   DOMAIN      131    262       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      340    409       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     139    146       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   436 AA;  50502 MW;  945D22AB398CECF2 CRC64;
     MNIFEKIKNQ LKSENPVNYN KFLKNLILDE DNSTSSHLII KAPNIFIATY IKRKYLPKIS
     VLYEKETGIK PNIEIITGKI KPKITNIEPI QTTTQISVLI PEYTFESFIV GPSNQFAYTA
     AKSVAENPGK NYNPLFIYGG VGLGKTHLLQ AIGNYLKNRL NVLYVTSEQF MNEFIENIRM
     KTPERFHEKY RNCDVLLIDD VQFFAGKEQT QEEFFHTFNE LYNQKKQICL TADRPPKKLY
     DLVDRLRSRF EAGLIVDIQP PELETKIEII RKKCELNGIY LPDEIIEYIA TKLDSNIREI
     EGMITKINAM SKILGVNEIT LDFAKQALKE HIKDKKENIT LEDIIELIAK EFNIKPSEIT
     SKSRNRNIVQ ARRCAIYLAR EFTQESTPKI ATYFGLKDHS AVSHAIKSFN KKLKEDSNFR
     MKIEELKSKI QLKKSE
//
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