GenomeNet

Database: UniProt
Entry: A1AV48_RUTMC
LinkDB: A1AV48_RUTMC
Original site: A1AV48_RUTMC 
ID   A1AV48_RUTMC            Unreviewed;       430 AA.
AC   A1AV48;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   25-OCT-2017, entry version 87.
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=Rmag_0001 {ECO:0000313|EMBL:ABL01805.1};
OS   Ruthia magnifica subsp. Calyptogena magnifica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria;
OC   sulfur-oxidizing symbionts; Candidatus Ruthia.
OX   NCBI_TaxID=413404 {ECO:0000313|EMBL:ABL01805.1, ECO:0000313|Proteomes:UP000002587};
RN   [1] {ECO:0000313|EMBL:ABL01805.1, ECO:0000313|Proteomes:UP000002587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cm {ECO:0000313|EMBL:ABL01805.1};
RX   PubMed=17303757; DOI=10.1126/science.1138438;
RA   Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA   Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA   Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A.,
RA   Cavanaugh C.M.;
RT   "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL   Science 315:998-1000(2007).
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:SAAS00911680}.
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; CP000488; ABL01805.1; -; Genomic_DNA.
DR   RefSeq; WP_011737431.1; NC_008610.1.
DR   ProteinModelPortal; A1AV48; -.
DR   STRING; 413404.Rmag_0001; -.
DR   EnsemblBacteria; ABL01805; ABL01805; Rmag_0001.
DR   KEGG; rma:Rmag_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235659; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000002587; 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:SF2; PTHR30050:SF2; 2.
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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002587};
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:UP000002587}.
FT   DOMAIN      121    254       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      337    406       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     129    136       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   430 AA;  48956 MW;  9CFF55D0C60739D2 CRC64;
     MSQTWSQCLN TLRDSIPLSQ YSVWIQPLKA LENNNTLSLL APNSQVLNYI NKHLKAQIKN
     AVAQHNKNLK IFISIASNQN TQQHITPLFE DYTFDNLILG NANQMAYGAT KQIAENIKTS
     PYNPFIIYGG SGLGKTHLMQ AAGHLSKEKN QNIKVIYVPL MDFVRNITSS LRHNTIENIK
     TFYQSADLLL VDDIHLIAGK EKSQEEFFHI FNFLFNGKKQ IIFTCDQSPK NIKSLENRLK
     TRFSQGLNLH LTPPELEMRA AILLKKSQNK RININLTEDT ALFIATHIAS NVRDLEGALL
     KLKAFVDFSK INHDFISKEI VETALGDLIK PQIKNIDIND IQKEVAKHYA LTISDLSSKS
     RKQHMVLARQ MAIFICHELS SLSLSKIGKH FGNRDHSTVL HAIKKIKEKH LENIEIKNDY
     ELIKLKLANL
//
DBGET integrated database retrieval system