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Database: UniProt
Entry: G7Z228_AZOL4
LinkDB: G7Z228_AZOL4
Original site: G7Z228_AZOL4 
ID   G7Z228_AZOL4            Unreviewed;       523 AA.
AC   G7Z228;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-SEP-2017, entry version 45.
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:CBS85431.1};
GN   OrderedLocusNames=AZOLI_0002 {ECO:0000313|EMBL:CBS85431.1};
OS   Azospirillum lipoferum (strain 4B).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS85431.1, ECO:0000313|Proteomes:UP000005667};
RN   [1] {ECO:0000313|Proteomes:UP000005667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H.,
RA   Robertson J.S., Barbe V., Calteau A., Rouy Z., Mangenot S.,
RA   Prigent-Combaret C., Normand P., Boyer M., Siguier P., Dessaux Y.,
RA   Elmerich C., Condemine G., Krishnen G., Kennedy I., Paterson A.H.,
RA   Gonzalez V., Mavingui P., Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(2011).
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}.
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DR   EMBL; FQ311868; CBS85431.1; -; Genomic_DNA.
DR   RefSeq; WP_014246506.1; NC_016622.1.
DR   STRING; 862719.AZOLI_0002; -.
DR   EnsemblBacteria; CBS85431; CBS85431; AZOLI_0002.
DR   KEGG; ali:AZOLI_0002; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000005667; 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:UP000005667};
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}.
FT   DOMAIN      220    348       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      431    500       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     228    235       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   523 AA;  58370 MW;  D9536CEEAC78C44F CRC64;
     MSVGVSLDQQ WARIRGRLKE EVGEIAYRSW LQPLSVASLV GGEVCIVVPT RFMRDWVLTH
     YADRIRALWS GENPEVQSID VIVASTNPPA ALVADNDDRD DDRAPPAPRS ADSRLDPRGF
     ESRPAPRPSR PSDAGSSAEP ASYYGNGSQA HQAPSTVYTS ASYGGASDES PNAVPAILED
     RSDLSAALDP RFTFENFVVG KPNELAHAAA RRVADATTVT FNPLFLYGGV GLGKTHLMHA
     LAWQIRKNDP NRKVLYLSAE KFMYQFIRAL RFKDTMAFKQ QFRSVDVLMI DDVQFISGKD
     STQEEFFHTF NALVDQNRQV IISADKSPSD LEGMEERLRS RLGWGLVADI HPTTYELRLG
     ILQAKADALQ ASIPLKVLEF LAHKITSNVR ELEGALNRIV AHAELVGRAI TLETTQEVLH
     DLLRANDRRV TIDEIQKRVA EHYNIRVADM HSARRARAVA RPRQIAMYLA KQLTARSLPE
     IGRKFGGRDH TTVMHAVKKV DELRATDPSF AEDVELLRRM LES
//
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