GenomeNet

Database: UniProt
Entry: Q1IVU4_KORVE
LinkDB: Q1IVU4_KORVE
Original site: Q1IVU4_KORVE 
ID   Q1IVU4_KORVE            Unreviewed;       461 AA.
AC   Q1IVU4;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   27-SEP-2017, entry version 95.
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   OrderedLocusNames=Acid345_0001 {ECO:0000313|EMBL:ABF39006.1};
OS   Koribacter versatilis (strain Ellin345).
OC   Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC   Candidatus Koribacter.
OX   NCBI_TaxID=204669 {ECO:0000313|EMBL:ABF39006.1, ECO:0000313|Proteomes:UP000002432};
RN   [1] {ECO:0000313|EMBL:ABF39006.1, ECO:0000313|Proteomes:UP000002432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin345 {ECO:0000313|EMBL:ABF39006.1,
RC   ECO:0000313|Proteomes:UP000002432};
RX   PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B.,
RA   Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J.,
RA   Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D.,
RA   Creasy T., Daugherty S.C., Davidsen T.M., DeBoy R.T., Detter J.C.,
RA   Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S.,
RA   Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C.,
RA   Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D.,
RA   Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L.,
RA   Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000360; ABF39006.1; -; Genomic_DNA.
DR   RefSeq; WP_011520808.1; NC_008009.1.
DR   ProteinModelPortal; Q1IVU4; -.
DR   STRING; 204669.Acid345_0001; -.
DR   EnsemblBacteria; ABF39006; ABF39006; Acid345_0001.
DR   KEGG; aba:Acid345_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; VENWVKD; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000002432; 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; 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   Complete proteome {ECO:0000313|Proteomes:UP000002432};
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:UP000002432}.
FT   DOMAIN      158    286       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      369    438       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     166    173       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   461 AA;  52019 MW;  4A14DBFD2DE3DD5A CRC64;
     MSLSTTTPPA PNPWLQVLDA LEKKVNRLSY DTWLKPTRFS HSQGNKIFVR VPTPEFRHIG
     EKYGDLIQEA LDSLGLGFED VEFVTDQAPA EAPMRHDGGF PPQSAAAPAP ARVQQARFDW
     DGAAQLNPKY IFDNFVTGPG NQFAHAASRA VADRPSKTYN PLFLYGGVGM GKTHLMQAIG
     HTIKRNNPEH SICYVSSEKF TNDMINSVRY DKMTSFRERY RTVDVLLIDD IQFIARKERT
     QEEFFHTFNA LHEQQKQLVI ASDRPPKELA EIEDRLRSRF EWGLIADIQP PDLETKVAIL
     QKKAESERTQ LPTDVALFIA SNIRSNVREL EGALIRLVAY SSLTGGELNL MTAQQVLKNI
     IDQQTRKVTI ESIQKACAEQ FGLRIAEIKA KNNSRAIVYP RQIAMYLAKH LTEASLPEIG
     RQFGGKHHTT VLHSVDKIDE ARKSDKDLNR LLNKLTESLS G
//
DBGET integrated database retrieval system