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Database: UniProt
Entry: I0R1P1_9MICO
LinkDB: I0R1P1_9MICO
Original site: I0R1P1_9MICO 
ID   I0R1P1_9MICO            Unreviewed;       505 AA.
AC   I0R1P1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   05-JUL-2017, entry version 37.
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=IMCC13023_02560 {ECO:0000313|EMBL:EIC91777.1};
OS   Candidatus Aquiluna sp. IMCC13023.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Luna cluster; Luna-1 subcluster; Candidatus Aquiluna.
OX   NCBI_TaxID=1081644 {ECO:0000313|EMBL:EIC91777.1, ECO:0000313|Proteomes:UP000054510};
RN   [1] {ECO:0000313|Proteomes:UP000054510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC13023 {ECO:0000313|Proteomes:UP000054510};
RX   PubMed=22689238; DOI=10.1128/JB.00586-12;
RA   Kang I., Lee K., Yang S.J., Choi A., Kang D., Lee Y.K., Cho J.C.;
RT   "Genome sequence of "Candidatus Aquiluna" sp. strain IMCC13023, a
RT   marine member of the Actinobacteria isolated from an arctic fjord.";
RL   J. Bacteriol. 194:3550-3551(2012).
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   -!- 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:EIC91777.1}.
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DR   EMBL; AJKR01000002; EIC91777.1; -; Genomic_DNA.
DR   EnsemblBacteria; EIC91777; EIC91777; IMCC13023_02560.
DR   PATRIC; fig|1081644.3.peg.260; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000054510; Unassembled WGS sequence.
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   Complete proteome {ECO:0000313|Proteomes:UP000054510};
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:UP000054510}.
FT   DOMAIN      198    343       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      410    479       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     206    213       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   505 AA;  57083 MW;  4BE725C66862CC1F CRC64;
     MFQSWNSATL TQSFPQALRV YAQIQISVQK SVHKYFKNLK ELQMADVALT VMWSDLVSKI
     ASDPRVTPHL KGHLDLAVPK GVLDDTLYLE VPNETTRSML QQRLKELLLD ALGEVAEYGG
     PTSFLIITNE ELKTPTRIEL AVEPEPLVID RDPATGPVPI TGSSGLNPKY SFDNFVTGGS
     NRFAHAASFA VAEAPAEAYN PLFIYGSSGL GKTHLLHAIG HYAMHLKPRT KVRYVSSEEF
     TNDFINAIQN NKTSEFQAQY RDVDILLVDD IQFLQGKDQT QEAFFHTFNN LHDHNKQVVI
     TSDLRPKQLE GFEERMLSRF EWGLITDIQA PEFETRVAIL RKKAALERIP VPDEVIEYMA
     TRISSNIREL EGTLIRVTAF ANLNRQPLDM DLVQTVLKDT YSVSEDTRIS PLEIIAATSS
     YFKITQEQLT GSGRQAAIAL ARQIAMHICR ELTDLSLPKI GTHFGNRDHT TVMYATKKIS
     SQMREKRYIY NQVSEIIQKI KDNHK
//
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