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Database: UniProt
Entry: A6NQD8_9FIRM
LinkDB: A6NQD8_9FIRM
Original site: A6NQD8_9FIRM 
ID   A6NQD8_9FIRM            Unreviewed;       426 AA.
AC   A6NQD8;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   16-JAN-2019, entry version 76.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:EDN01743.1};
GN   ORFNames=BACCAP_00408 {ECO:0000313|EMBL:EDN01743.1};
OS   Pseudoflavonifractor capillosus ATCC 29799.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Pseudoflavonifractor.
OX   NCBI_TaxID=411467 {ECO:0000313|EMBL:EDN01743.1, ECO:0000313|Proteomes:UP000003639};
RN   [1] {ECO:0000313|EMBL:EDN01743.1, ECO:0000313|Proteomes:UP000003639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDN01743.1,
RC   ECO:0000313|Proteomes:UP000003639};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H.,
RA   Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDN01743.1, ECO:0000313|Proteomes:UP000003639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDN01743.1,
RC   ECO:0000313|Proteomes:UP000003639};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M.,
RA   Liep D., Gordon J.;
RT   "Draft genome sequence of Pseudoflavonifractor capillosus ATCC
RT   29799.";
RL   Submitted (JUN-2007) 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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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:EDN01743.1}.
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DR   EMBL; AAXG02000004; EDN01743.1; -; Genomic_DNA.
DR   ProteinModelPortal; A6NQD8; -.
DR   STRING; 411467.BACCAP_00408; -.
DR   EnsemblBacteria; EDN01743; EDN01743; BACCAP_00408.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   Proteomes; UP000003639; 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   Gene3D; 3.30.300.180; -; 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; IPR038454; DnaA_N_sf.
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:SAAS00756129};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000003639};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003639}.
FT   DOMAIN      119    247       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      331    400       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     127    134       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      400    420       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   426 AA;  48731 MW;  2CFB50868406FB37 CRC64;
     MEADMTATAI NTWFDDCTAV ALEEDRFVIH SPTNFKRDII RKRYVPNIQK ALHELFAADF
     QVEVLGEGEL DHFTEASKPV DSTFLPGTED YTFERFVVGS SNKFAHAAAL SVAENPGKSY
     NPLFIYGESG LGKTHLLYAI AHKIHATRPD FRVVYIKGDA FTNELIQAIR EGSNQEFREK
     FRSADVFLMD DVQFIAGRES SQEEMFHTFN TLYEAGRQIV FTADRPPKEM LRLDDRLKTR
     FEWGLPVDIK PPDYETRVAI IKNKAIRRGM ELPEPVLQYI AENITSNVRQ IEGTVNKILA
     FQELMGESVD VDTVTRAVRD MFKEKAEFLP SADVIIEEVC KFYNIENDAL RGQGRTKDTA
     LARQMAMYLI RRMTSLSLKE IGKEFEGRDH TTVMHSIERI ENLMKSNAEV AEIIKDLNAN
     INARYE
//
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