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Database: UniProt
Entry: A0A0P6WP02_9CHLR
LinkDB: A0A0P6WP02_9CHLR
Original site: A0A0P6WP02_9CHLR 
ID   A0A0P6WP02_9CHLR        Unreviewed;       451 AA.
AC   A0A0P6WP02;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   25-OCT-2017, entry version 16.
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=ADM99_15375 {ECO:0000313|EMBL:KPL70505.1};
OS   Leptolinea tardivitalis.
OC   Bacteria; Chloroflexi; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Leptolinea.
OX   NCBI_TaxID=229920 {ECO:0000313|EMBL:KPL70505.1, ECO:0000313|Proteomes:UP000050430};
RN   [1] {ECO:0000313|EMBL:KPL70505.1, ECO:0000313|Proteomes:UP000050430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YMTK-2 {ECO:0000313|EMBL:KPL70505.1,
RC   ECO:0000313|Proteomes:UP000050430};
RA   Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT   "Genome sequence of Leptolinea tardivitalis DSM 16556.";
RL   Submitted (JUL-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|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:SAAS00911680}.
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:KPL70505.1}.
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DR   EMBL; LGCK01000014; KPL70505.1; -; Genomic_DNA.
DR   RefSeq; WP_062422401.1; NZ_LGCK01000014.1.
DR   EnsemblBacteria; KPL70505; KPL70505; ADM99_15375.
DR   PATRIC; fig|229920.5.peg.443; -.
DR   Proteomes; UP000050430; 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   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: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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000050430};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
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:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050430}.
FT   DOMAIN      145    272       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      353    422       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     153    160       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   451 AA;  50941 MW;  7813CF8CC0B20DAA CRC64;
     MMNPQSAWQA ALGQLQMEMP KANFDTWVRS TELINYEKNT FTVGVQNAYA RDWLDTRLTS
     TVSRILTGLM DSSQSVNFVV WQKNIEPAVD EAVIENEIEE EQREIEVRTN RTLNPRYTFD
     SFVVGASNRL AHAASLAVAE NPARAYNPLF LYGGVGLGKT HMLQAIGNST NARNLSVLYV
     SSEDFTNDLI NAIRTHTTNQ FRDRYRKADI LLIDDIQFIA GKESTQEEFF HTFNALHGAN
     KQLVISSDRP PKAMVTLEER LRSRFEWGLT VDIQPPDLET RMAILRSKAE RAGRRVPNEI
     IEIIARQIQS NIRELEGALT RVLAFSDLSG MPLTTQLVTS ALADMLPQHS SMEPRQVVNT
     VARAFGVTTE QMLGRDRSRG VALPRQVAMY LLREVANVSL PQIGQALGGR DHTTVMYACE
     KVADMIERDD HFRRQVVQLR DQLFGRTPMA L
//
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