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Database: UniProt
Entry: F3YV49_DESAF
LinkDB: F3YV49_DESAF
Original site: F3YV49_DESAF 
ID   F3YV49_DESAF            Unreviewed;       454 AA.
AC   F3YV49;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   25-OCT-2017, entry version 48.
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=Desaf_0001 {ECO:0000313|EMBL:EGJ48367.1};
OS   Desulfovibrio africanus str. Walvis Bay.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ48367.1, ECO:0000313|Proteomes:UP000007844};
RN   [1] {ECO:0000313|EMBL:EGJ48367.1, ECO:0000313|Proteomes:UP000007844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ48367.1};
RX   PubMed=21642452; DOI=10.1128/JB.05223-11;
RA   Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M.,
RA   Brandt C.C., Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S.,
RA   Han J., Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L.,
RA   Palumbo A.V., Elias D.A.;
RT   "Genome sequence of the mercury-methylating and pleomorphic
RT   Desulfovibrio africanus Strain Walvis Bay.";
RL   J. Bacteriol. 193:4037-4038(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:SAAS00911680}.
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; CP003221; EGJ48367.1; -; Genomic_DNA.
DR   RefSeq; WP_014258249.1; NC_016629.1.
DR   STRING; 690850.Desaf_0001; -.
DR   EnsemblBacteria; EGJ48367; EGJ48367; Desaf_0001.
DR   KEGG; daf:Desaf_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000007844; 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: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:UP000007844};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
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:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007844}.
FT   DOMAIN      150    289       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      363    431       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     158    165       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   454 AA;  50814 MW;  3A1A5B6084A620E1 CRC64;
     MNETWQQITQ ILEKELNPNQ FTLWIKPLHA SLNNNVLELA APNEFVAAWV RDKLTTHISQ
     AALQVLGSPS TVTVRSTPKP TPSAPETATK PSSAESTVTV KAKHLGLPLT TPLQSTQCCN
     WRHSFDDFVV GPSNDLAYAA AQGVVRNDFS PGPLFISSSA GLGKTHLIQA IGHAAQDRTR
     SKSLTLRYLT AEEFATKMLM ALNAKDMSRF KTQFREGIDI LLLEDIHFLQ GKAMFQDELL
     STIKALQERG SRVVFTSSFL PKELSNVDTH LVSRFCSGFL TVIDMPDFDM RRRIVQHKSR
     QLQVNVPDDV AELLAESITC DIRQLESCLQ NLVLKARLLN ERISLDMARD VLGNYASQNS
     GMALERIVEM VCRTFILSPT QLASKSRKRN IVLARNTAFF LARKHTQLSL KDIADRFNRT
     HSTVIKGITS LELEMSKKTP AGRQIQRTLE QMDL
//
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