GenomeNet

Database: UniProt
Entry: E3D7Q4_GARV3
LinkDB: E3D7Q4_GARV3
Original site: E3D7Q4_GARV3 
ID   E3D7Q4_GARV3            Unreviewed;       535 AA.
AC   E3D7Q4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-SEP-2017, entry version 48.
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   ECO:0000313|EMBL:ADP38212.1};
GN   OrderedLocusNames=HMPREF0421_20126 {ECO:0000313|EMBL:ADP38212.1};
OS   Gardnerella vaginalis (strain ATCC 14019 / 317).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Gardnerella.
OX   NCBI_TaxID=525284 {ECO:0000313|EMBL:ADP38212.1, ECO:0000313|Proteomes:UP000001453};
RN   [1] {ECO:0000313|EMBL:ADP38212.1, ECO:0000313|Proteomes:UP000001453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14019 / 317 {ECO:0000313|Proteomes:UP000001453};
RX   PubMed=20865041; DOI=10.1371/journal.pone.0012411;
RA   Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M.,
RA   Sutton G., Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X.,
RA   Gibbs R.A., Leigh S.R., Stumpf R., White B.A., Highlander S.K.,
RA   Nelson K.E., Wilson B.A.;
RT   "Comparative genomics of Gardnerella vaginalis strains reveals
RT   substantial differences in metabolic and virulence potential.";
RL   PLoS ONE 5:E12411-E12411(2010).
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:SAAS00731907}.
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002104; ADP38212.1; -; Genomic_DNA.
DR   RefSeq; WP_004114028.1; NC_014644.1.
DR   RefSeq; YP_003985235.1; NC_014644.1.
DR   ProteinModelPortal; E3D7Q4; -.
DR   EnsemblBacteria; ADP38212; ADP38212; HMPREF0421_20126.
DR   GeneID; 9903662; -.
DR   KEGG; gvg:HMPREF0421_20126; -.
DR   PATRIC; fig|525284.18.peg.122; -.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; VENWVKD; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000001453; 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:SF12; PTHR30050:SF12; 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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001453};
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   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001453}.
FT   DOMAIN      223    362       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      438    507       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     231    238       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   535 AA;  59606 MW;  DD845CAD15D6BE87 CRC64;
     MSEAFEDPSA QAAIVWSNTL AVLRHNALLS NRDKSWFESV KPEAIFGTTI VLCVSNIETQ
     QALQNELSSA LLTSLKICTG KDMFPAFKII QNSEKENNNT LQNVSNTSKT SQSLDNTTNN
     NSDSSDSNDS SDPKKVESFL DDSYDSIPVQ KDFDYATGLK TMQNTNLNVQ SINQKQTNIP
     ASVNRDPTTH LNTYATFDTF VPGDSNRFAR TVALAVAEGS GRDFNPLCIY GGSGLGKTHL
     LNAIGNYALV KDSSLKVRYI TSEEFTNEFI EALQNTSQNQ GQIANFNRRY REVDVLLIDD
     IQFLGGKEAT LEQFFHTFNA LYQANKRIVI ASDVAPKNLR GFESRLISRF ESGLTVDIKP
     PDLETRIAIL RMMASMNGSN VPSDVLDLIA ERFTENIREL EGALTRVTAV ASLSNQPVSK
     ALAEQALQDF FASDIEVRPT DIIGQVAQYF HMTFDEMVGR SRTKNVALAR QIAMYLAREM
     TSMSLVDIGE VFGGRDHTTV MHAYTRISGE MQEKQEIYNY VMELTVRLKQ NPSKK
//
DBGET integrated database retrieval system