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Database: UniProt
Entry: M5QPD0_9PSED
LinkDB: M5QPD0_9PSED
Original site: M5QPD0_9PSED 
ID   M5QPD0_9PSED            Unreviewed;       502 AA.
AC   M5QPD0;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   25-OCT-2017, entry version 35.
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   ECO:0000313|EMBL:EMI09140.1};
GN   ORFNames=B195_01005 {ECO:0000313|EMBL:EMI09140.1};
OS   Pseudomonas sp. Lz4W.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1206777 {ECO:0000313|EMBL:EMI09140.1, ECO:0000313|Proteomes:UP000011925};
RN   [1] {ECO:0000313|EMBL:EMI09140.1, ECO:0000313|Proteomes:UP000011925}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lz4W {ECO:0000313|EMBL:EMI09140.1,
RC   ECO:0000313|Proteomes:UP000011925};
RX   PubMed=23788547;
RA   Pandiyan A., Ray M.K.;
RT   "Draft Genome Sequence of the Antarctic Psychrophilic Bacterium
RT   Pseudomonas syringae Strain Lz4W.";
RL   Genome Announc. 1:E00377-13(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: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}.
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:EMI09140.1}.
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DR   EMBL; AOGS01000001; EMI09140.1; -; Genomic_DNA.
DR   RefSeq; WP_003437978.1; NZ_AOGS01000001.1.
DR   EnsemblBacteria; EMI09140; EMI09140; B195_01005.
DR   GeneID; 29351258; -.
DR   PATRIC; fig|1206777.3.peg.204; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000011925; 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   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:UP000011925};
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:UP000011925}.
FT   DOMAIN      199    404       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      410    479       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     207    214       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   502 AA;  56229 MW;  A1BA6731F8281458 CRC64;
     MSVELWQQCV ELLRDELPAQ QFNTWIRPLQ VEAEGDELRV YAPNRFVLDW VNEKYLSRLL
     ELLNEHSNGM APALSLLIGS KRSSAPRAAP NAPLAAAASQ QAPAPASAPT ASAPASAPAP
     KQSAQASEEP SRASFDPMAG ASSQQAPVRA EQRTVQVEGA LKHTSYLNRT FTFENFVEGK
     SNQLARAAAW QVADNPKHGY NPLFLYGGVG LGKTHLMHAV GNHLLKKNPN AKVVYLHSER
     FVADMVKALQ LNAINEFKRF YRSVDALLID DIQFFARKER SQEEFFHTFN ALLEGGQQVI
     LTSDRYPKEI EGLEERLKSR FGWGLTVAVE PPELETRVAI LMKKADQAKV DLPHDAAFFI
     AQRIRSNVRE LEGALKRVIA HSHFMGRDIT IELIRESLKD LLALQDKLVS VDNIQRTVAE
     YYKIKISDLL SKRRSRSVAR PRQVAMALSK ELTNHSLPEI GDVFGGRDHT TVLHACRKIN
     ELKESDADIR EDYKNLLRTL TT
//
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