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Database: UniProt
Entry: E1VRJ7_GLUAR
LinkDB: E1VRJ7_GLUAR
Original site: E1VRJ7_GLUAR 
ID   E1VRJ7_GLUAR            Unreviewed;       478 AA.
AC   E1VRJ7;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   05-JUL-2017, entry version 57.
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:CBT74250.1};
GN   OrderedLocusNames=AARI_00010 {ECO:0000313|EMBL:CBT74250.1};
OS   Glutamicibacter arilaitensis (strain DSM 16368 / CIP 108037 / IAM
OS   15318 / JCM 13566 / Re117) (Arthrobacter arilaitensis).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae;
OC   Glutamicibacter.
OX   NCBI_TaxID=861360 {ECO:0000313|EMBL:CBT74250.1, ECO:0000313|Proteomes:UP000006878};
RN   [1] {ECO:0000313|EMBL:CBT74250.1, ECO:0000313|Proteomes:UP000006878}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC   {ECO:0000313|Proteomes:UP000006878};
RX   PubMed=21124797; DOI=10.1371/journal.pone.0015489;
RA   Monnet C., Loux V., Gibrat J.F., Spinnler E., Barbe V., Vacherie B.,
RA   Gavory F., Gourbeyre E., Siguier P., Chandler M., Elleuch R.,
RA   Irlinger F., Vallaeys T.;
RT   "The Arthrobacter arilaitensis Re117 genome sequence reveals its
RT   genetic adaptation to the surface of cheese.";
RL   PLoS ONE 5:E15489-E15489(2010).
RN   [2] {ECO:0000313|Proteomes:UP000006878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC   {ECO:0000313|Proteomes:UP000006878};
RA   Genoscope.;
RT   "Complete genome sequence of Arthrobacter arilaitensis (strain DSM
RT   16368 / CIP 108037 / JCM 13566 / Re117).";
RL   Submitted (JUL-2010) 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: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}.
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DR   EMBL; FQ311875; CBT74250.1; -; Genomic_DNA.
DR   RefSeq; WP_013347404.1; NC_014550.1.
DR   STRING; 861360.AARI_00010; -.
DR   EnsemblBacteria; CBT74250; CBT74250; AARI_00010.
DR   KEGG; aai:AARI_00010; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000006878; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006878};
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:UP000006878}.
FT   DOMAIN      169    300       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      381    450       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     177    184       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      450    477       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   478 AA;  53697 MW;  40DB78AE3684E9AD CRC64;
     MSSDETNSIG SSWRQVIRKI EDDDRVKARY RAFVSLAKPQ GLIGTTLLVA VPNDLTRDIL
     QTQLREPLDE ALREVFQDDI RCAVSVDLSL SDELEEDEQE TKPAPPAAPA VVEAPGPRPQ
     PAPQPTPPSN SQEFGRLNPK YIFDTFVIGS SNRFAHAAAV AVAEAPAKAY NPLFIYGDSG
     LGKTHLLHAI GHYARHLYKG IRVRYVNSEE FTNDFINSIR DDEGASFKQT YRNVDILLID
     DIQFLANKDA TQEEFFHTFN ALHNHNKQVV ITSDLPPKQL QGFEDRMRSR FEWGLLTDIQ
     PPELETRIAI LRKKADAENL SAPGDVMEYI ASRISTNIRE LEGALIRVTA FASLNNQPVD
     LALAETVLKD LISEDGAQEI TPSTIIKQTA EYFGLSIDEL NSKSRTRTLV TARQIAMYLL
     RELTDMSLPK IGAELGGRDH TTVIHADRKI RELMAERRAI FNQVTELTNR IKQSQREH
//
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