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Database: UniProt
Entry: A0A098G0J5_9GAMM
LinkDB: A0A098G0J5_9GAMM
Original site: A0A098G0J5_9GAMM 
ID   A0A098G0J5_9GAMM        Unreviewed;       453 AA.
AC   A0A098G0J5;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   05-JUL-2017, entry version 23.
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:CEG55489.1};
GN   ORFNames=LFA_0001 {ECO:0000313|EMBL:CEG55489.1};
OS   Legionella fallonii LLAP-10.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=1212491 {ECO:0000313|EMBL:CEG55489.1, ECO:0000313|Proteomes:UP000032430};
RN   [1] {ECO:0000313|EMBL:CEG55489.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LLAP-10 {ECO:0000313|EMBL:CEG55489.1};
RA   GOMEZ-VALERO Laura;
RL   Submitted (SEP-2014) 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; LN614827; CEG55489.1; -; Genomic_DNA.
DR   RefSeq; WP_045094368.1; NZ_LN614827.1.
DR   EnsemblBacteria; CEG55489; CEG55489; LFA_0001.
DR   KEGG; lfa:LFA_0001; -.
DR   KO; K02313; -.
DR   Proteomes; UP000032430; 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:UP000032430};
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   ECO:0000313|EMBL:CEG55489.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032430}.
FT   DOMAIN      150    359       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      361    430       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     158    165       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   453 AA;  51402 MW;  4615B02BE1985DA7 CRC64;
     MSATVWQKCL GLLQDEYSAQ QFNTWLRPLQ VHTDEQRLIL LAPNRFVVDW VKKHFFSRIE
     ELINQFCGDD IKSVSIEIGS KPSESTPGSS PDTTVSISGA PAVKASVKKT VDYKSSHLNK
     KFVFDSFVEG NSNQLARAAS MQVAERPGDA YNPLFIYGGV GLGKTHLMHA IGNNILKNNP
     EAKVLYLHSE RFVADMVKAL QTNSINEFKR FYRSLNALLI DDIQFFAGKD RSQEEFFHTF
     NALLEGQQQI ILTSDRYPKE IEGMEERLKS RFGWGLTVAV EPPELETRVA ILISKAEQSN
     IELPYEVAFF IAKRIRSNVR ELEGALRRVI ANAHFTGKPI TIEFVHEALR DLLALQDKLV
     TIENIQKTVA EYYKVKVADL LSKRRSRSIA RPRQMAMALS KELTNHSLPE IGDHFGGRDH
     TTVIHACRKV KELIQDDSDF AEDYKNLMRI LSS
//
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