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Database: UniProt
Entry: R5JNY9_9BACE
LinkDB: R5JNY9_9BACE
Original site: R5JNY9_9BACE 
ID   R5JNY9_9BACE            Unreviewed;       181 AA.
AC   R5JNY9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   12-APR-2017, entry version 22.
DE   SubName: Full=Chromosomal replication initiator protein dnaA {ECO:0000313|EMBL:CCY50517.1};
GN   ORFNames=BN523_02543 {ECO:0000313|EMBL:CCY50517.1};
OS   Bacteroides sp. CAG:189.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides; environmental samples.
OX   NCBI_TaxID=1262737 {ECO:0000313|EMBL:CCY50517.1, ECO:0000313|Proteomes:UP000018406};
RN   [1] {ECO:0000313|EMBL:CCY50517.1, ECO:0000313|Proteomes:UP000018406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:189 {ECO:0000313|Proteomes:UP000018406};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA   Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA   Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA   Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA   Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA   Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA   Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA   Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA   MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA   Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units
RT   of genetic variation.";
RL   Submitted (NOV-2012) 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|SAAS:SAAS00735475}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00756131}.
CC   -!- SIMILARITY: Belongs to the DnaA family.
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:CCY50517.1}.
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DR   EMBL; CAYI010000119; CCY50517.1; -; Genomic_DNA.
DR   Proteomes; UP000018406; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:InterPro.
DR   CDD; cd06571; Bac_DnaA_C; 1.
DR   Gene3D; 1.10.1750.10; -; 1.
DR   InterPro; IPR001957; Chromosome_initiator_DnaA.
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:SF12; PTHR30050:SF12; 1.
DR   Pfam; PF00308; Bac_DnaA; 1.
DR   Pfam; PF08299; Bac_DnaA_C; 1.
DR   SMART; SM00760; Bac_DnaA_C; 1.
DR   SUPFAM; SSF48295; SSF48295; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS01008; DNAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|SAAS:SAAS00747556};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018406};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|SAAS:SAAS00747534};
KW   DNA-binding {ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00747535};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018406}.
FT   DOMAIN       86    155       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
SQ   SEQUENCE   181 AA;  20463 MW;  65AC3E1D55D12684 CRC64;
     MVAELEKPTV ELRKNILRNK IHRDGLQFPP EVIDYIAENV NESVRDLEGI VIAIMARSTI
     FNKEIDLDLA QHIVRGVVRN ETKSISIDDI INTVCKHFGL ETNAIHTKSR KREVVQARQV
     AMYLAKTYTD FSTSKIGKFI GNKDHATVLH ACKTVKGQCE VDKGFRADLE TIESSLKKKN
     S
//
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