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Database: UniProt
Entry: A0A0A7I5L9_9BIFI
LinkDB: A0A0A7I5L9_9BIFI
Original site: A0A0A7I5L9_9BIFI 
ID   A0A0A7I5L9_9BIFI        Unreviewed;       525 AA.
AC   A0A0A7I5L9;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   25-OCT-2017, entry version 25.
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=AH67_00005 {ECO:0000313|EMBL:AIZ15533.1};
OS   Bifidobacterium pseudolongum PV8-2.
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=1447715 {ECO:0000313|EMBL:AIZ15533.1, ECO:0000313|Proteomes:UP000030636};
RN   [1] {ECO:0000313|EMBL:AIZ15533.1, ECO:0000313|Proteomes:UP000030636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PV8-2 {ECO:0000313|EMBL:AIZ15533.1,
RC   ECO:0000313|Proteomes:UP000030636};
RX   PubMed=25614573;
RA   Vazquez-Gutierrez P., Lacroix C., Chassard C., Klumpp J.,
RA   Stevens M.J., Jans C.;
RT   "Bifidobacterium pseudolongum Strain PV8-2, Isolated from a Stool
RT   Sample of an Anemic Kenyan Infant.";
RL   Genome Announc. 3:0-0(2015).
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}.
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DR   EMBL; CP007457; AIZ15533.1; -; Genomic_DNA.
DR   RefSeq; WP_039170667.1; NZ_CP007457.1.
DR   EnsemblBacteria; AIZ15533; AIZ15533; AH67_00005.
DR   KEGG; bpsp:AH67_00005; -.
DR   KO; K02313; -.
DR   Proteomes; UP000030636; Chromosome.
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; IPR000253; FHA_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   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.
DR   PROSITE; PS50006; FHA_DOMAIN; 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:UP000030636};
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:UP000030636}.
FT   DOMAIN      319    377       FHA. {ECO:0000259|PROSITE:PS50006}.
FT   NP_BIND     221    228       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   525 AA;  58223 MW;  EDF3F4F4AA7A01A9 CRC64;
     MSGDNLDPGT QSALIWSNAL TLLRGNATLS ARQKGWFEGV LPEAIYGTTI ILAVENNETQ
     RMLQTDLNSV LLQALKVANG GIELFPAFKI LQSSTRATPP GAQVEAERAP SRAKPTAAEA
     APRGSAAPAK PATHYDEAVV QTFEDIMPGT NFDMPASTGS FPQVPMKDRQ RKPSLDPETH
     LNRNDTFDTF VPGDSNRFAR TVALAVAEGS GQDFNPLCIY GGSGLGKTHL LNAIGNYALL
     KQPGTRVRYV TSEEFTNEFI DSLRADKASG ESRINEFNRK YREIDVLLID DIQFLGDKES
     TLEQFFHTFN SLYQNNKRIV IASDVPPKNL KGFESRLISR FEQGLTVDVK PPDLETRIAI
     LRMLVSTNGT YVPNDVLDLI AERFTDNIRE LEGALNRVTA LASLNNQPVT RILAEQTLQD
     FFSTDIELKP TDIIGRVAKY FHLTFDDLVG PTRTKNVTIA RQIAMYLTRD LTSMSLVNIG
     QVFGGRDHTT VMHNCKTISE GMKDNPQIYT YVTELTLQLR QRISE
//
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