GenomeNet

Database: UniProt
Entry: C8WXS7_ALIAD
LinkDB: C8WXS7_ALIAD
Original site: C8WXS7_ALIAD 
ID   C8WXS7_ALIAD            Unreviewed;       454 AA.
AC   C8WXS7;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   27-SEP-2017, entry version 66.
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=Aaci_0001 {ECO:0000313|EMBL:ACV57066.1};
OS   Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC
OS   27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 /
OS   104-1A) (Bacillus acidocaldarius).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Alicyclobacillus.
OX   NCBI_TaxID=521098 {ECO:0000313|EMBL:ACV57066.1, ECO:0000313|Proteomes:UP000001917};
RN   [1] {ECO:0000313|Proteomes:UP000001917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 /
RC   NRRL B-14509 / 104-1A {ECO:0000313|Proteomes:UP000001917};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Ovchinnikova G., Chertkov O., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Klenk H.-P.,
RA   Eisen J.A.;
RT   "The complete chromosome of Alicyclobacillus acidocaldarius subsp.
RT   acidocaldarius DSM 446.";
RL   Submitted (SEP-2009) 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: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; CP001727; ACV57066.1; -; Genomic_DNA.
DR   RefSeq; WP_012809465.1; NC_013205.1.
DR   ProteinModelPortal; C8WXS7; -.
DR   STRING; 521098.Aaci_0001; -.
DR   EnsemblBacteria; ACV57066; ACV57066; Aaci_0001.
DR   KEGG; aac:Aaci_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000001917; 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:UP000001917};
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:UP000001917}.
FT   DOMAIN      148    276       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      360    429       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     156    163       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   454 AA;  52004 MW;  2485D96A2CCF61B8 CRC64;
     MMSTKVDPTY DALWNQVLQM VQDKVSGPTY STWFEDTHIV RIDESEQTVY ISAPSTFVRN
     WLSEHYTSLV ETLMMTLMDR EYRVRFITED DVQAPAVIVR RAPEPVTAEE DTETNLNPRY
     TFDSFVIGAG NRFAHAACLA VAERPANAYN PLFIYGGVGL GKTHLMHAIG HYVRQHYPNF
     KVSYISSERF TNEFIAAIRD KNPDSFRARY RTVDVLLIDD IQFIANKEQT QEEFFHTFNS
     LHEVGKQIVI SSDRPPREIP TLEDRLRSRF EWGLITDIQP PDLETRIAIL QRKAKADGLD
     VPVDVLAFIA NQIDSNIREL EGALTRVIAY SSLVKEDLSV ALAEEALKDL IHPNRPRAVT
     VNHVQKVVAD HYGLKVDDLK GKKRTRNIAF PRQIAMYLTR ELTDLSLPRI GEAFGGRDHT
     TVMHACERVH EEMMRDDELR ATIERLSQAI RTLT
//
DBGET integrated database retrieval system