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DNAA_TERTT
ID   DNAA_TERTT              Reviewed;         593 AA.
AC   C5BKL9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN   Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377}; OrderedLocusNames=TERTU_0002;
OS   Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Teredinibacter.
OX   NCBI_TaxID=377629;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39867 / T7901;
RX   PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA   Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA   Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA   Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA   Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA   Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA   Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA   Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT   "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT   endosymbiont of marine wood-boring bivalves (shipworms).";
RL   PLoS ONE 4:E6085-E6085(2009).
CC   -!- FUNCTION: Plays an important role in the initiation and regulation of
CC       chromosomal replication. Binds to the origin of replication; it binds
CC       specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-
CC       TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
CC       {ECO:0000255|HAMAP-Rule:MF_00377}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00377}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00377}.
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DR   EMBL; CP001614; ACR12930.1; -; Genomic_DNA.
DR   RefSeq; WP_015819043.1; NC_012997.1.
DR   AlphaFoldDB; C5BKL9; -.
DR   SMR; C5BKL9; -.
DR   STRING; 377629.TERTU_0002; -.
DR   PRIDE; C5BKL9; -.
DR   EnsemblBacteria; ACR12930; ACR12930; TERTU_0002.
DR   KEGG; ttu:TERTU_0002; -.
DR   eggNOG; COG0593; Bacteria.
DR   HOGENOM; CLU_026910_0_0_6; -.
DR   OMA; AGKEHTQ; -.
DR   OrthoDB; 219876at2; -.
DR   Proteomes; UP000009080; 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   Gene3D; 3.40.50.300; -; 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; Cytoplasm; DNA replication; DNA-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..593
FT                   /note="Chromosomal replication initiator protein DnaA"
FT                   /id="PRO_1000205664"
FT   REGION          97..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         298..305
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   593 AA;  66583 MW;  D607D96D2D6FC1DA CRC64;
     MSDPCWEQCV SCLQNELPSQ QFNTWIRPLR VEESSTLLLR LIAPNRFVQD WVNDKYRTRI
     EEIISNSDAG PKSLEIAVAQ RARAGFEVVR NAKVAPAVPV PDPLPSTGRD ESSFQPPKGN
     TSADYSGHSD LGFQSPHRRQ SPFSESQERF TQPLEMSRFG SGRPSNERSN EGAIGGSTES
     SADRERIPLQ GVVEDLFKPT KNSNDFVEPR STDPLLEIES RPIIETVSPR DIQDFGSQLT
     SRVKKKDVEG GIQHKHNLNT TFIFDNFVVG KSNQLGLAAA SQVAENPGGA YNPLFIYGGV
     GLGKTHLMHA VGNALVQRKP GARVVYLHSE RFVADMVKAL QLNAISDFKR FYRSVDALLI
     DDIQFFAGKE RSQEEFFHTF NALLEGGQQI ILTCDKYPKE INGLEERLKS RFGWGLTVAI
     EPPELETRVA ILKRKAESSR MPLPDDAAFF IAQRIRSNVR ELEGALKRVI ANAQFTQRSI
     SVELVREALK DLLALQDRLV SIDNIQRVVA EYYKIKVSDL HSKRRSRSVA RPRQVAMYLA
     KDLTHHSLPE IGDAFGGRDH TTVLHACRKI RDLQESDADI REDVKNLLRT LTT
 
 
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