GenomeNet

Database: UniProt
Entry: A0A0F6WA68_9DELT
LinkDB: A0A0F6WA68_9DELT
Original site: A0A0F6WA68_9DELT 
ID   A0A0F6WA68_9DELT        Unreviewed;       534 AA.
AC   A0A0F6WA68;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-SEP-2017, entry version 17.
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   ORFNames=DB32_008491 {ECO:0000313|EMBL:AKF11342.1};
OS   Sandaracinus amylolyticus.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Sorangiineae; Sandaracinaceae; Sandaracinus.
OX   NCBI_TaxID=927083 {ECO:0000313|EMBL:AKF11342.1, ECO:0000313|Proteomes:UP000034883};
RN   [1] {ECO:0000313|EMBL:AKF11342.1, ECO:0000313|Proteomes:UP000034883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 53668 {ECO:0000313|EMBL:AKF11342.1,
RC   ECO:0000313|Proteomes:UP000034883};
RA   Sharma G., Subramanian S.;
RT   "Genome assembly of Sandaracinus amylolyticus DSM 53668.";
RL   Submitted (MAR-2015) 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; CP011125; AKF11342.1; -; Genomic_DNA.
DR   RefSeq; WP_053238217.1; NZ_CP011125.1.
DR   EnsemblBacteria; AKF11342; AKF11342; DB32_008491.
DR   KEGG; samy:DB32_008491; -.
DR   KO; K02313; -.
DR   Proteomes; UP000034883; 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:UP000034883};
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:UP000034883}.
FT   DOMAIN      227    373       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      441    510       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     235    242       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   534 AA;  59452 MW;  C039FE460C2500C7 CRC64;
     MDGLWESTLG RLRGRLAEET YATWLEPIRF DGIEGRIVRL RIPNRFFADW ISARYLPDIL
     ESLAALTGAE GLDVSWVVDP SLQEQVTSAG QVASPAVADR EVASTGVMLA PGAMLADEAM
     LSRGARMAAA GRVTARASRP PVRALRAAGE LPFDVEGGAD RAPIARPPVA RSVAADRVAP
     PVESGSPVGE QSYALNPRYL FDNFVVGPSN QLAHAASIAA SSSPGKRYNP LFIYSKVGLG
     KTHLVNAVGH RVLEDRRDAR VLFLSAERFT NEFIWALQHK RIDEFRARYR GSCDVLVIDD
     IQFLAGREQT QEEFFHTFNA LYHADKQIVV TSDVYPQHIP EMQERLISRF QWGLVADIQA
     PELDTRIAIL RKKAEQEQLH LGDDVALLVA QVVQSNVREL EGTLLRLAVL ADAQQRPLDI
     ELARMALGAH QPKGRDARQT SVEDIQRAAC EYFQIGIKEL MSDRRHRNVS LPRMIAMYIC
     RERLDLSYPM IGARFGNKDH TTVMNAHRKI SGLVESDERV KRAIEVIERK VGIS
//
DBGET integrated database retrieval system