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Database: UniProt
Entry: A0A240A3P4_SERFI
LinkDB: A0A240A3P4_SERFI
Original site: A0A240A3P4_SERFI 
ID   A0A240A3P4_SERFI        Unreviewed;       443 AA.
AC   A0A240A3P4;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   13-FEB-2019, entry version 12.
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:SNV78062.1};
GN   ORFNames=SAMEA4384070_00001 {ECO:0000313|EMBL:SNV78062.1};
OS   Serratia ficaria.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=61651 {ECO:0000313|EMBL:SNV78062.1, ECO:0000313|Proteomes:UP000215134};
RN   [1] {ECO:0000313|EMBL:SNV78062.1, ECO:0000313|Proteomes:UP000215134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC12148 {ECO:0000313|EMBL:SNV78062.1,
RC   ECO:0000313|Proteomes:UP000215134};
RG   Pathogen Informatics;
RL   Submitted (JUN-2017) 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: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}.
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DR   EMBL; LT906479; SNV78062.1; -; Genomic_DNA.
DR   BioCyc; GCF_900187015:CKW09_RS00005-MONOMER; -.
DR   Proteomes; UP000215134; Chromosome 1.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000215134};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215134}.
FT   DOMAIN      140    342       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      351    420       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     148    155       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      302    322       {ECO:0000256|SAM:Coils}.
FT   COILED      420    440       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   443 AA;  49755 MW;  F1B72B85815F2760 CRC64;
     MWIRPLQAEL SDNTLALYAP NRFVLDWVRD KYLNNINGLL NDFCGTDAPL LRFEVGSKPI
     TQMISQTVTA SVSSSSAPAA PVARAAAPSR PSWDNAAPQP ELSYRSNVNP KHTFDNFVEG
     KSNQLARAAA RQVADNPGGA YNPLFLYGGT GLGKTHLLHA VGNGIMARKA NAKVVYMHSE
     RFVQDMVKAL QNNAIEEFKR YYRSVDALLI DDIQFFANKE RSQEEFFHTF NALLEGNQQI
     ILTSDRYPKE INGVEDRLKS RFGWGLTVAI EPPELETRVA ILMKKADEND IRLPGEVAFF
     IAKRLRSNVR ELEGALNRVI ANANFTGRAI TIDFVREALR DLLALQEKLV TIDNIQKTVA
     EYYKIKVADL LSKRRSRSVA RPRQMAMALA KELTNHSLPE IGDAFGGRDH TTVLHACRKI
     EQLREESHDI KEDFSNLIRT LSS
//
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