GenomeNet

Database: UniProt
Entry: M1FAU9_9ALTE
LinkDB: M1FAU9_9ALTE
Original site: M1FAU9_9ALTE 
ID   M1FAU9_9ALTE            Unreviewed;       491 AA.
AC   M1FAU9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   20-JUN-2018, entry version 39.
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   ECO:0000313|EMBL:AFP28939.1};
GN   ORFNames=MRBBS_0001 {ECO:0000313|EMBL:AFP28939.1};
OS   Marinobacter sp. BSs20148.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Marinobacter.
OX   NCBI_TaxID=490759 {ECO:0000313|EMBL:AFP28939.1, ECO:0000313|Proteomes:UP000011757};
RN   [1] {ECO:0000313|EMBL:AFP28939.1, ECO:0000313|Proteomes:UP000011757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSs20148 {ECO:0000313|EMBL:AFP28939.1};
RX   PubMed=23682144;
RA   Song L., Ren L., Li X., Yu D., Yu Y., Wang X., Liu G.;
RT   "Complete Genome Sequence of Marinobacter sp. BSs20148.";
RL   Genome Announc. 1:E00236-13(2013).
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:SAAS00747961}.
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; CP003735; AFP28939.1; -; Genomic_DNA.
DR   EnsemblBacteria; AFP28939; AFP28939; MRBBS_0001.
DR   KEGG; mbs:MRBBS_0001; -.
DR   PATRIC; fig|490759.3.peg.1; -.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000011757; 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   Gene3D; 3.30.300.180; -; 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; IPR038454; DnaA_N_sf.
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   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:UP000011757};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00747973};
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:SAAS00748008};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011757}.
FT   DOMAIN      188    316       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      399    468       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     196    203       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   491 AA;  55829 MW;  105C6E42CE62965D CRC64;
     MQRFVIRWCR YGMWQQCLEV LRDEFPAQQF NTWLRPLQPD LRDGQLVLFA PNRFVMDWVN
     EKYLRRIEEI LKELNGGHAP RVGMKVGSAP KAGDSERREP TAINTNPLAK DDRGELANQQ
     SRPAAPVTAP AASRPRTSGT RPGAQIEGDI KHQSFLNETF TFQTFVEGKS NQLARAASMQ
     VAENPGGAYN PLFLYGGVGL GKTHLMHAVG NEIVRRNPNA KVAYLRSERF VADMVKALQL
     NAINEFKRYY RSVDALLIDD IQFFARKERS QEEFFHTFNA LLEGGQQVIV TSDRFPKEIV
     DLEERLKSRF GWGLTVMVEP PELETRVAIL MKKAEQVNVK LSSEAAFFIA QKIRSNVREL
     EGALRLVIAN AHFTGSEITP PFIRESLKDL LALHEKQVSI DNIQRTVAEY YKIKVADLHS
     KRRTRNVTRP RQVAMSLSKE LTNHSLPEIG GAFGGRDHTT VLHACKKIVE LQESDPSIRE
     DYQNFMRLLT S
//
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