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Database: UniProt
Entry: F0SUG9_SYNGF
LinkDB: F0SUG9_SYNGF
Original site: F0SUG9_SYNGF 
ID   F0SUG9_SYNGF            Unreviewed;       446 AA.
AC   F0SUG9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   05-JUL-2017, entry version 46.
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   OrderedLocusNames=Sgly_0001 {ECO:0000313|EMBL:ADY54382.1};
OS   Syntrophobotulus glycolicus (strain DSM 8271 / FlGlyR).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Syntrophobotulus.
OX   NCBI_TaxID=645991 {ECO:0000313|EMBL:ADY54382.1, ECO:0000313|Proteomes:UP000007488};
RN   [1] {ECO:0000313|Proteomes:UP000007488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488};
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA   Chertkov O., Held B., Detter J.C., Tapia R., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Syntrophobotulus glycolicus DSM 8271.";
RL   Submitted (FEB-2011) 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}.
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DR   EMBL; CP002547; ADY54382.1; -; Genomic_DNA.
DR   RefSeq; WP_013623253.1; NC_015172.1.
DR   STRING; 645991.Sgly_0001; -.
DR   EnsemblBacteria; ADY54382; ADY54382; Sgly_0001.
DR   KEGG; sgy:Sgly_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000007488; 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:UP000007488};
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:UP000007488}.
FT   DOMAIN      141    269       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      353    422       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     149    156       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   446 AA;  51468 MW;  A4580981D2C7BF8F CRC64;
     MSPNSTYLNA FWENILDKLR NELSKASFDT WLSSTKLVSF VNNRLTISVS NEFAKDWLES
     RYSALIKSTV QNYLNRPVAL TFVVEQEQNY QPEIIESNDQ KFGILSHPLN RKYTFDTFVI
     GNGNRFAHAA ALAVAESPAK SYNPLFLYGG SGLGKTHLMH AIGHIINRNF PEMKIVYVTG
     EQFTNEMIDS IRYERQVEFR NTYRKVDLLL IDDIQFLAGK EGTQEEFFHT FNTLYEANKQ
     IIISSDRPPR EIPTLEERLR SRFEWGLTTD INPPDYETRI AILRKKAQLE NYIVPDEIIT
     FIASSIQSNI RELEGALSKI TAFCMLTNQS ITVELAEEIL KDMIPNRNQK IISIELIQKT
     VAEHYKMSVN ELKQKKRTRT IAFPRQVAMY ISRQLTDCSL PQIGEKFGGR DHTTVIHAFD
     KISEMKEHDP FVEKSINEII NKIKST
//
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