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Database: UniProt
Entry: A0A0J5GF97_9NEIS
LinkDB: A0A0J5GF97_9NEIS
Original site: A0A0J5GF97_9NEIS 
ID   A0A0J5GF97_9NEIS        Unreviewed;       481 AA.
AC   A0A0J5GF97;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   25-OCT-2017, entry version 18.
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   ORFNames=ACG97_11295 {ECO:0000313|EMBL:KMJ52848.1};
OS   Vogesella sp. EB.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Vogesella.
OX   NCBI_TaxID=1526735 {ECO:0000313|EMBL:KMJ52848.1, ECO:0000313|Proteomes:UP000054352};
RN   [1] {ECO:0000313|EMBL:KMJ52848.1, ECO:0000313|Proteomes:UP000054352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EB {ECO:0000313|EMBL:KMJ52848.1,
RC   ECO:0000313|Proteomes:UP000054352};
RA   Arrua Day P., Revale S., Alvarez H.M.;
RT   "Genome wide analysis of metabolism in the polyhydroxybutyrate-
RT   producing Vogesella sp. strain EB.";
RL   Submitted (JUN-2015) 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: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:KMJ52848.1}.
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DR   EMBL; LFDT01000018; KMJ52848.1; -; Genomic_DNA.
DR   RefSeq; WP_047967467.1; NZ_LFDT01000018.1.
DR   EnsemblBacteria; KMJ52848; KMJ52848; ACG97_11295.
DR   PATRIC; fig|1526735.3.peg.2410; -.
DR   Proteomes; UP000054352; 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:UP000054352};
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:UP000054352}.
FT   DOMAIN      178    307       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      389    458       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     186    193       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   481 AA;  53212 MW;  2620DBD40DA68761 CRC64;
     MTEPENFWPA CLTRLEEELS SQQFNTWIRP LSAEAGDEGV VLYAPNRFIL QFIKDRFLAR
     IEALAIELLG EVSVELRIGA AAGAPVAVAR PAPASSAPRS NGTPAASVDV ESAVAKVAAN
     APAVAPTAKQ TAVKAIGGGH ESTRLNPSFT FDTLVTGKGN QLARAAAMQI AENPGDPAYN
     PLFVYGGVGL GKTHLIQAIG NHVYLKNPQA KIRYIHAERY VADIMRAYQH KAFDEFKRYY
     HSLDLLLIDD IQFFAGKNRT QEEFFYAFNA LIEGGKQVIM TCDSYPKQIE GMEERLISRF
     SWGLTVEIQP PELEMRVAIL MKKAEADNTK LDHNVAFFIA QNVRSNVREL EGALKRVVAY
     ARFSNQSITM ELVKEALKDI LAAGNRQVTI ETIQKTVADY YKIKLSDMHS KKRSRDIARP
     RQVAMTLAKE LTSLSLPNIG DAFGGRDHTT VLHACKTIAE MRGNDSEIAH DYDTLLAMLR
     N
//
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