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Database: UniProt
Entry: A9WR29_RENSM
LinkDB: A9WR29_RENSM
Original site: A9WR29_RENSM 
ID   A9WR29_RENSM            Unreviewed;       467 AA.
AC   A9WR29;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   25-OCT-2017, entry version 84.
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:ABY21761.1};
GN   OrderedLocusNames=RSal33209_0001 {ECO:0000313|EMBL:ABY21761.1};
OS   Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484
OS   / NBRC 15589 / NCIMB 2235).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae;
OC   Renibacterium.
OX   NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY21761.1, ECO:0000313|Proteomes:UP000002007};
RN   [1] {ECO:0000313|Proteomes:UP000002007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC   {ECO:0000313|Proteomes:UP000002007};
RX   PubMed=18723615; DOI=10.1128/JB.00721-08;
RA   Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S.,
RA   Chen D.S., Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J.,
RA   Burd H., Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT   "Genome sequence of the fish pathogen Renibacterium salmoninarum
RT   suggests reductive evolution away from an environmental Arthrobacter
RT   ancestor.";
RL   J. Bacteriol. 190:6970-6982(2008).
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}.
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DR   EMBL; CP000910; ABY21761.1; -; Genomic_DNA.
DR   RefSeq; WP_012243469.1; NC_010168.1.
DR   ProteinModelPortal; A9WR29; -.
DR   STRING; 288705.RSal33209_0001; -.
DR   EnsemblBacteria; ABY21761; ABY21761; RSal33209_0001.
DR   KEGG; rsa:RSal33209_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000002007; 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:UP000002007};
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:UP000002007}.
FT   DOMAIN      158    288       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      370    439       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     166    173       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   467 AA;  52525 MW;  F9E8A439E2AE0BB1 CRC64;
     MNTESNGDIA GSWRKVVKIL EQDEHVSPRQ RGFITLAQAQ GLIGSTLLLA VPNELTREVL
     QNQIKGSLDL ALREVFGEDV LCAISIDTDL TPVPEEVRQE VEPDEPSEES RPQPGPPSTS
     NEFGRLNPKY LFDTFVIGQS NRFAHAAAVA VAEAPAKAYN PLFIYGDSGL GKTHLLHAIG
     HYARRLYNGI RVRYVNSEEF TNEFINSIRY DEGTSFKTTY RNVDILLIDD IQFLSGKEAT
     QEEFFHTFNA LHNHNKQVVI TSDLPPKQLS GFEERMRSRF EWGLLTDVQP PELETRIAIL
     RKKAIGEGLH APDDVLEYIA SKISTNIREL EGALIRVTAF ASLNRQSVDV GLTETVLKDL
     ITDNGDQQIT AATILGQTSA YFKLSLDELR SKSRTRTLVN ARQIAMYLCR ELTDLSLPKI
     GQELGGRDHT TVIHADRKIR ELMAERRTIF NQVTELTNLI RQQQREG
//
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