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Database: UniProt
Entry: R6Z2F0_9BACT
LinkDB: R6Z2F0_9BACT
Original site: R6Z2F0_9BACT 
ID   R6Z2F0_9BACT            Unreviewed;       487 AA.
AC   R6Z2F0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   25-OCT-2017, entry version 31.
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=BN590_01654 {ECO:0000313|EMBL:CDD24632.1};
OS   Alistipes sp. CAG:29.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes; environmental samples.
OX   NCBI_TaxID=1262694 {ECO:0000313|EMBL:CDD24632.1, ECO:0000313|Proteomes:UP000018138};
RN   [1] {ECO:0000313|EMBL:CDD24632.1, ECO:0000313|Proteomes:UP000018138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:29 {ECO:0000313|Proteomes:UP000018138};
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|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:CDD24632.1}.
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DR   EMBL; CBGS010000061; CDD24632.1; -; Genomic_DNA.
DR   Proteomes; UP000018138; 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:UP000018138};
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:UP000018138}.
FT   DOMAIN      183    313       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      394    463       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     191    198       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   487 AA;  55082 MW;  9618FF8485EE0637 CRC64;
     MQNYSQLCHI KNSATLIMLN NTQTYSDMWQ NCLDRIKAQT SEEEFVKWFQ PIVPLEFDGT
     NLRLRVPNES YVHQIEKNYI PFLRPIISQL YGQQTRLHYA VPRSTPPAVP VTADADTTAI
     SRFNTQTNTA NIKNPFVIPG LKKIIIDPQL NPGLTFATFI EGECNRLARS AGMSVAVNPG
     NNPFNPLYIY GDSGLGKTHI VQAIGHEVRQ RHPELQVLYV SMNKFQAQFQ TAYKNGEIPD
     FIHFYQMIDV LIIDDIQELT GKTGTQNAFF NIFNHLQLAG KQLILTSDKP PVELKDIEQR
     LLTRFKWGLS AQLNTPDYDT KLKIIRVKAQ KFGAQISDDV VAYLADNISA NVREIEGALS
     SLVANASFLG RKITTSLAKE ILKVYVQLYQ KEITLDHIIE VVCEYLNLDF ARFNSTERTR
     EIAQARQIAM YLAKQHTKAP LTTIGAAIGG RNHATVLHSC KAVSNLIETD KAFRRQVEEI
     EKKVLAQ
//
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