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Database: UniProt
Entry: K5YJF2_9PSED
LinkDB: K5YJF2_9PSED
Original site: K5YJF2_9PSED 
ID   K5YJF2_9PSED            Unreviewed;       482 AA.
AC   K5YJF2;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   16-JAN-2019, entry version 43.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:EKM95368.1};
GN   ORFNames=C211_13691 {ECO:0000313|EMBL:EKM95368.1};
OS   Pseudomonas sp. Chol1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=440512 {ECO:0000313|EMBL:EKM95368.1, ECO:0000313|Proteomes:UP000008490};
RN   [1] {ECO:0000313|EMBL:EKM95368.1, ECO:0000313|Proteomes:UP000008490}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Chol1 {ECO:0000313|EMBL:EKM95368.1,
RC   ECO:0000313|Proteomes:UP000008490};
RX   PubMed=23405354;
RA   Holert J., Alam I., Larsen M., Antunes A., Bajic V.B., Stingl U.,
RA   Philipp B.;
RT   "Genome Sequence of Pseudomonas sp. Strain Chol1, a Model Organism for
RT   the Degradation of Bile Salts and Other Steroid Compounds.";
RL   Genome Announc. 1:E00014-12(2013).
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:SAAS00756121}.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EKM95368.1}.
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DR   EMBL; AMSL01000076; EKM95368.1; -; Genomic_DNA.
DR   RefSeq; WP_008569097.1; NZ_AMSL01000076.1.
DR   EnsemblBacteria; EKM95368; EKM95368; C211_13691.
DR   PATRIC; fig|440512.3.peg.2694; -.
DR   Proteomes; UP000008490; 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; 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 {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756129};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008490};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   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}.
FT   DOMAIN      179    309       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      390    459       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     187    194       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   482 AA;  54483 MW;  E696253560FA31AB CRC64;
     MSVELWQQCV DLLRDELPTQ QFNTWIRPLQ VESEGDELRV YAPNRFVLDW VNEKYLSRLL
     ELLTERADGM TPALSLLIGS KRTAPAALPS AAAARQQMAV PVVTIADATS VTPMEQAATT
     VAEPEPEVAR PTRNVQVEGG LKHTSYLNRT FTFENFVEGK SNQLARAAAW QVADNPKHGY
     NPLFLYGGVG LGKTHLMHAV GNHLLKKNPN AKVVYLHSER FVADMVKALQ LNAINEFKRF
     YRSVDALLID DIQFFAKKER SQEEFFHTFN ALLEGGQQVI LTSDRYPKEI DGLEERLKSR
     FGWGLTVAVE PPELETRVAI LMKKADQAKV DLPHDAAFFI AQRIRSNVRE LEGALKRVIA
     HAHFMGREIT IELIRESLKD LLALQDKLVS VDNIQRTVAE YYKIKVADLL SKRRSRSVAR
     PRQVAMALSK ELTNHSLPEI GDAFGGRDHT TVLHACRKIA ELREIDADIR EDYKNLLRTL
     TT
//
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