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Database: UniProt
Entry: A0A140L750_9THEO
LinkDB: A0A140L750_9THEO
Original site: A0A140L750_9THEO 
ID   A0A140L750_9THEO        Unreviewed;       449 AA.
AC   A0A140L750;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   25-OCT-2017, entry version 13.
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_3 {ECO:0000313|EMBL:KXG76375.1};
GN   Synonyms=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=AN618_16150 {ECO:0000313|EMBL:KXG76375.1};
OS   Fervidicola ferrireducens.
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Fervidicola.
OX   NCBI_TaxID=520764 {ECO:0000313|EMBL:KXG76375.1, ECO:0000313|Proteomes:UP000070427};
RN   [1] {ECO:0000313|EMBL:KXG76375.1, ECO:0000313|Proteomes:UP000070427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y170 {ECO:0000313|EMBL:KXG76375.1,
RC   ECO:0000313|Proteomes:UP000070427};
RA   Patel B.K.;
RT   "Draft genome sequnece of Fervidicola ferrireducens strain Y170.";
RL   Submitted (DEC-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:KXG76375.1}.
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DR   EMBL; LOED01000020; KXG76375.1; -; Genomic_DNA.
DR   RefSeq; WP_066353750.1; NZ_LOED01000020.1.
DR   EnsemblBacteria; KXG76375; KXG76375; AN618_16150.
DR   PATRIC; fig|520764.3.peg.1732; -.
DR   Proteomes; UP000070427; 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:UP000070427};
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:UP000070427}.
FT   DOMAIN      144    272       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      356    425       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     152    159       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   449 AA;  51152 MW;  FF1C072CAC45D901 CRC64;
     MTHNLPDLWQ QVLKVLSSEL NNDVSFNTFL KPTKLLGIED DIAIVEVPND FLKEVLEKRY
     SNLLKDILSS ILNRNVSIFF KIDSSSGSEQ ASTVDAIEKD TKNYNEEIQC NLNSKYTFDT
     FVVGNSNRFA HAASLAVAQA PAKAYNPLFI YGGVGLGKTH LMHAIGHYIL EHNPSSKVMY
     VSSEKFTNEL INSIRDDKNV EFRNKYRNID VLLIDDIQFI AGKERTQEEF FHTFNALYEA
     NKQIIISSDR PPKEIPTLEE RLRSRFEWGL ITDIQPPDFE TRIAILRKKA MMEKLTVPDE
     VINFIATKIE TNIRELEGAL IRIVAFSSLT NKPIDLALAE HVLKDILPNS KPKSVSVMDI
     LQVVGNYFSV KIEDFKSKKR TKEIAYARQV AMYLCRELTD FSLPKIGEEF GGRDHTTVIH
     ACEKISRDIQ KDPQFASLIE NLKKKILSG
//
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