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Database: UniProt
Entry: A0A091BXC2_9ENTE
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ID   A0A091BXC2_9ENTE        Unreviewed;       444 AA.
AC   A0A091BXC2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-SEP-2017, entry version 25.
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=TMU3MR103_2190 {ECO:0000313|EMBL:KFN89140.1};
OS   Tetragenococcus muriaticus 3MR10-3.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Tetragenococcus.
OX   NCBI_TaxID=1302648 {ECO:0000313|EMBL:KFN89140.1, ECO:0000313|Proteomes:UP000029381};
RN   [1] {ECO:0000313|EMBL:KFN89140.1, ECO:0000313|Proteomes:UP000029381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3MR10-3 {ECO:0000313|EMBL:KFN89140.1,
RC   ECO:0000313|Proteomes:UP000029381};
RA   Chuea-nongthon C., Rodtong S., Yongsawatdigul J., Steele J.L.,
RA   Liu X.-y., Speers J., Glasner J.D., Neeno-Eckwall E.C.;
RT   "Genome sequence of Tetragenococcus muriaticus.";
RL   Submitted (AUG-2014) 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:SAAS00756131}.
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:KFN89140.1}.
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DR   EMBL; JPVT01000244; KFN89140.1; -; Genomic_DNA.
DR   RefSeq; WP_028790049.1; NZ_JPVT01000244.1.
DR   EnsemblBacteria; KFN89140; KFN89140; TMU3MR103_2190.
DR   PATRIC; fig|1302648.3.peg.2143; -.
DR   Proteomes; UP000029381; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:SF12; PTHR30050:SF12; 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:SAAS00731922};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029381};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Hydrolase {ECO:0000313|EMBL:KFN89140.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029381}.
FT   DOMAIN      140    271       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      352    421       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     148    155       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      414    444       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   444 AA;  50729 MW;  690DDB44DCB66CDB CRC64;
     MPSLETIWKE LQESYRKEMN PVSYNTWIEP AKPISFYDNQ LIIEVPTTVQ KNYWEKNLAG
     KILETFFMMS GEEILPTFVT PDEAESYKQE EPKEEENTPK FPEHKTMLNS KYTFDTFVIG
     KGNQMAHAAA LVTAEDPGAI YNPLFFYGGV GLGKTHLMQA IGHQMLEIHP TAKVKYVSSE
     NFTNDFINSI QNNKMEEFRN EYRTMDLLLV DDVQFLVNKE GTQEEFFNTF EELYRNNKQI
     VLTSDRLPNE IPNLPKRLVS RFAWGLSVDI TPPDLETRTA ILRKKAEAEN LEIPDDTLSY
     IAGQIDSNIR ELEGALVRVQ AYAAIQSSDI TTSLAAEALK ALKVGTNLSQ LTVEQILEKV
     AEYYHINTTD LTGKKRTKGI VVPRQIAMYL CRNLTDYSLP KIGAEFGGKD HTTVIHAYEK
     VNQLLEENET IKNEVKEIKN LLME
//
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