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Database: UniProt
Entry: A4XN60_PSEMY
LinkDB: A4XN60_PSEMY
Original site: A4XN60_PSEMY 
ID   A4XN60_PSEMY            Unreviewed;       494 AA.
AC   A4XN60;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   05-JUL-2017, entry version 76.
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=Pmen_0001 {ECO:0000313|EMBL:ABP82776.1};
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739 {ECO:0000313|EMBL:ABP82776.1, ECO:0000313|Proteomes:UP000000229};
RN   [1] {ECO:0000313|EMBL:ABP82776.1, ECO:0000313|Proteomes:UP000000229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ymp {ECO:0000313|Proteomes:UP000000229};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C.,
RA   Bruce D., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Hersman L., Dubois J., Maurice P.,
RA   Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) 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; CP000680; ABP82776.1; -; Genomic_DNA.
DR   STRING; 399739.Pmen_0001; -.
DR   EnsemblBacteria; ABP82776; ABP82776; Pmen_0001.
DR   KEGG; pmy:Pmen_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235659; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000000229; 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:UP000000229};
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:UP000000229}.
FT   DOMAIN      191    396       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      402    471       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     199    206       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   494 AA;  55330 MW;  9C9747375FA4FEED CRC64;
     MELWQQCVEL LRDELPAQQF NTWIRPLQVE AEGDELRVYA PNRFVLDWVN EKYLSRLLEL
     LGERAGGLVP ALSLLIGSKR AATARVAPTA PLPAAARAAQ VQAAATASKP VPPPAQEEPS
     RASFDSMAGA APQPPTPAVA PRAERTVQVE GGLKHTSYLN RTFTFDNFVE GKSNQLARAA
     AWQVADNPKH GYNPLFLYGG VGLGKTHLMH AVGNHLLAKN PNAKVVYLHS ERFVADMVKA
     LQLNAINEFK RFYRSVDALL IDDIQFFAKK ERSQEEFFHT FNALLEGGQQ VILTSDRYPK
     EIEGLEERLK SRFGWGLTVA VEPPELETRV AILMKKADQA KVELPHDAAF FIAQRIRSNV
     RELEGALKRV IAHSHFMGRD ITIELIRESL KDLLALQDKL VSIDNIQRTT AEYYKIKISD
     LLSKRRSRSI ARPRQVAMAL SKELTNHSLP EIGVAFGGRD HTTVLHACRK IAELRESDAD
     IREDYKNLLR TLTT
//
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