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Database: UniProt
Entry: G8AFE1_AZOBR
LinkDB: G8AFE1_AZOBR
Original site: G8AFE1_AZOBR 
ID   G8AFE1_AZOBR            Unreviewed;       518 AA.
AC   G8AFE1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   05-JUL-2017, entry version 44.
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:CCC96490.1};
GN   ORFNames=AZOBR_10277 {ECO:0000313|EMBL:CCC96490.1};
OS   Azospirillum brasilense Sp245.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=1064539 {ECO:0000313|EMBL:CCC96490.1, ECO:0000313|Proteomes:UP000007319};
RN   [1] {ECO:0000313|EMBL:CCC96490.1, ECO:0000313|Proteomes:UP000007319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sp245 {ECO:0000313|EMBL:CCC96490.1,
RC   ECO:0000313|Proteomes:UP000007319};
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; HE577327; CCC96490.1; -; Genomic_DNA.
DR   RefSeq; WP_014238812.1; NC_016617.1.
DR   STRING; 1064539.AZOBR_10277; -.
DR   EnsemblBacteria; CCC96490; CCC96490; AZOBR_10277.
DR   KEGG; abs:AZOBR_10277; -.
DR   PATRIC; fig|192.7.peg.255; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000007319; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
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:UP000007319};
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:UP000007319}.
FT   DOMAIN      215    343       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      426    495       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     223    230       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   518 AA;  57294 MW;  5DFF6DCA0292F4B5 CRC64;
     MSVGASLDQQ WARIRGRLKD EVGEIAYRSW LQPLSFAGIR GGEVRIVVPT RFMRDWVLTH
     YADRIRNLWA GENPDVLSID VVVASANAPS MLMPELTSDG DAGEPSRDSD PVDGAAGGGP
     VPPAPAPRAA ALNQSASYGA ASYGANSYIG SSYSAGPPSF ASDESPTAVA SVLEDRTDIS
     APLDPRFTFE NFVVGKPNEL AHAAARRVAD ATSVTFNPLF LYGGVGLGKT HLMHAIAWQI
     RRNDPNRKVI YLSAEKFMYQ FIRALRFKDT MAFKQQFRSV DVLMIDDVQF ISGKDSTQEE
     FFHTFNALVD QNRQVIISAD KSPSDLEGME ERLRSRLGWG LVADIHPTTY ELRLGILQAK
     ADALNAAIPL KVLEFLAHKI TSNVRELEGA LNRIVAHAEL VGRAISLEST QEVLHDLLRA
     NDRRVTIDEI QKRVAEHFNI RVADMHSARR ARAVARPRQV AMYLAKQLTA RSLPEIGRKF
     GGRDHTTVMH AVKKVEELRT TDPAFAEDVE LLRRMLES
//
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