GenomeNet

Database: UniProt
Entry: A0A109UGC3_9FIRM
LinkDB: A0A109UGC3_9FIRM
Original site: A0A109UGC3_9FIRM 
ID   A0A109UGC3_9FIRM        Unreviewed;       458 AA.
AC   A0A109UGC3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-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};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=AOC36_00005 {ECO:0000313|EMBL:AMC92430.1};
OS   Erysipelothrix larvae.
OC   Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Erysipelothrix.
OX   NCBI_TaxID=1514105 {ECO:0000313|EMBL:AMC92430.1, ECO:0000313|Proteomes:UP000063781};
RN   [1] {ECO:0000313|EMBL:AMC92430.1, ECO:0000313|Proteomes:UP000063781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LV19 {ECO:0000313|EMBL:AMC92430.1,
RC   ECO:0000313|Proteomes:UP000063781};
RA   Lim S., Kim B.-C.;
RT   "Erysipelothrix larvae sp. LV19 isolated from the larval gut of the
RT   rhinoceros beetle, Trypoxylus dichotomus.";
RL   Submitted (OCT-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:SAAS00735475}.
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP013213; AMC92430.1; -; Genomic_DNA.
DR   RefSeq; WP_067629592.1; NZ_CP013213.1.
DR   EnsemblBacteria; AMC92430; AMC92430; AOC36_00005.
DR   KEGG; erl:AOC36_00005; -.
DR   KO; K02313; -.
DR   Proteomes; UP000063781; Chromosome.
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; 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   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:UP000063781};
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:UP000063781}.
FT   DOMAIN      150    281       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      367    436       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     158    165       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   458 AA;  51807 MW;  78D2E2A84512B6DF CRC64;
     MNNAKFSYLD SVWNQTKNTI KSEGKVDNSI YTTYFEHSSL VDLNDSKAWI TVPSFLHKVV
     LSDGLDIINT ALCSILSRDK IDSEVFVESE YEPEQHDQPL ETVNIEPIKP KVINTDGISD
     SQTFDNFVVG TSNKEAHAAA LACAYRPGQF YTPLFIHGNS GLGKTHLLNS IGNYVKKNHA
     DSQIYYTSSV DFVRQVAESI GKNQIEDFKN QMYDLDVLLI DDIQFLAGKE KSHEIFFHIF
     NELAYRKKQI VITSDRPPTE IKGLEERLIS RFSSGLTVGM DSPEFETSLA ILEMKIRNQS
     VDPSIFDEEV LHYIASNFSK DVRQLEGALN RLLFFSIEFS KSDHVAMDTA ISAFKKSGIE
     STTREITPKL IKQIVSDYYG LTVTQLTGKS RTKAISNARH IAIYLTRKFL DMPYNKIGNE
     FGRRDHSTII NACDKIENAI NSDQYLASAI QEIELKIK
//
DBGET integrated database retrieval system