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Database: UniProt
Entry: A0A087EGN3_9BIFI
LinkDB: A0A087EGN3_9BIFI
Original site: A0A087EGN3_9BIFI 
ID   A0A087EGN3_9BIFI        Unreviewed;       601 AA.
AC   A0A087EGN3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   20-DEC-2017, entry version 28.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=BITS_1497 {ECO:0000313|EMBL:KFJ06934.1};
OS   Bifidobacterium tsurumiense.
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=356829 {ECO:0000313|EMBL:KFJ06934.1, ECO:0000313|Proteomes:UP000029080};
RN   [1] {ECO:0000313|EMBL:KFJ06934.1, ECO:0000313|Proteomes:UP000029080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13495 {ECO:0000313|EMBL:KFJ06934.1,
RC   ECO:0000313|Proteomes:UP000029080};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-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:SAAS00735475}.
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:KFJ06934.1}.
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DR   EMBL; JGZU01000006; KFJ06934.1; -; Genomic_DNA.
DR   RefSeq; WP_026642506.1; NZ_JGZU01000006.1.
DR   EnsemblBacteria; KFJ06934; KFJ06934; BITS_1497.
DR   Proteomes; UP000029080; 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; 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   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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029080};
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:UP000029080}.
FT   DOMAIN      288    427       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      503    572       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     296    303       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      455    475       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   601 AA;  66513 MW;  FE5EA446F3FFA907 CRC64;
     MASEPNDPGT QAALVWADTL RILRSNNSLT ARDKGWFEGV SPEAIFGTTI VLCVTNPSAQ
     QALQGQLSSF LAAALKMTTG QDMFPAFKII PPAEPMVSDE TVSQQSPVTD TRIDTNSNPN
     DLQTGSDFNA FDSAPTSMPQ NRDERAGSGS AERPISSAYS QEVPEIQSNR TSGYQSAPEN
     SAYQPYPNQN VNSVNSAEQY HDSYSDYPYS DNSYPSATHE TQPGSQRNAA PNSSGSADQQ
     FSANTYKAAL DPKTHLNTNA TFDTFVPGDS NRFARTVALA VAEGSGRDFN PLCIYGGSGL
     GKTHLLNAIG NYALVRDHNL KVRYVTSEEF TNEFIEALQT PNKSQGLIAD FNRRYREVDV
     LLIDDIQFLG GKESTLEQFF HTFNALYQAN KRIVIASDVA PKNLKGFEAR LISRFESGLT
     VDVKPPDLET RIAILRMMAS MNHSNIPNDV LDLIAERFTE NIRELEGALN RVTAIASLSN
     QPVSRAQAEQ TLQDFFSTDV EIKPTDIIGQ VAKYFHLTFD DLVGRSRTKN VAMARQVSMY
     LAREMTSMSL VDIGEVFGGR DHTTVMHAYT RISNEMQEKQ EIYNYVMELT VQLKQNPRRQ
     D
//
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