(data stored in SCRATCH zone)

SWISSPROT: A4F5N2_SACEN

ID   A4F5N2_SACEN            Unreviewed;       592 AA.
AC   A4F5N2;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   11-DEC-2019, entry version 97.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:CAL99356.1};
GN   OrderedLocusNames=SACE_0001 {ECO:0000313|EMBL:CAL99356.1};
GN   ORFNames=A8924_0383 {ECO:0000313|EMBL:PFG93155.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99356.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99356.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99356.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93155.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93155.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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; AM420293; CAL99356.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93155.1; -; Genomic_DNA.
DR   RefSeq; WP_009945727.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0001; -.
DR   EnsemblBacteria; CAL99356; CAL99356; SACE_0001.
DR   KEGG; sen:SACE_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; ATHIERN; -.
DR   OrthoDB; 219876at2; -.
DR   BioCyc; SERY405948:SACE_RS00005-MONOMER; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
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   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; 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   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;
DR   PRODOM; A4F5N2.
DR   SWISS-2DPAGE; A4F5N2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756129};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   DOMAIN          283..411
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          495..564
FT                   /note="Bac_DnaA_C"
FT                   /evidence="ECO:0000259|SMART:SM00760"
FT   NP_BIND         291..298
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
FT   REGION          88..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..147
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..248
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   592 AA;  65800 MW;  58FC14DA3F77EDD8 CRC64;
     MADHQADLGR VWEEVVQELS SGTLSPQQRA WMRVTRPIGL LDGTALLAAP SDFAKEAIER
     ALREPITDAL SRRLGRDVSL AVKVDTAVQA PSRPAPPPAE SWPTRDSITG PDRPTGFAEA
     GVSPYISTSS SYLQPPRTDS FTPPVTGSLP AVDNHYPTAE QPRVVDYQSA DYPTTEYHDW
     PTAAELTAGT PHEGESEAAP ESDDEVDEER EAIDAANEIW PTFGRGQAPE AQQGQPFTAP
     KHAPPTSQTR LNAKYTFDTF VIGASNRFAH AAAVAAAEAP ARAYNPLFIW GESGLGKTHL
     LHAVGHYAQR LFPGMRVRYV STEEFTNDFI NSLRDDRQVA FQRRYRDVDV LLVDDIQFLE
     GKEGTQEEFF HTFNTLHNSN KQIVVSSDRP PKGLRTLEDR LRTRFEWGLI TDIQPPELET
     RIAILRKKAA QDRMNAPADV LEFIAARIER NIRELEGALI RVTAFASLNR QPVDVQLAEI
     VLRDLIPDSQ TPEITAPTIM AVTADFFSVT IDDLCGPGKT KALAQARQIA MYLCRELTDS
     SLPKIGQSFG GRDHTTVMHA DKKIRKEMAE RRRVYDQVQE LTSRIKQQSR GS
//

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