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Database: UniProt
Entry: F9MQU0_9FIRM
LinkDB: F9MQU0_9FIRM
Original site: F9MQU0_9FIRM 
ID   F9MQU0_9FIRM            Unreviewed;       498 AA.
AC   F9MQU0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   05-JUL-2017, entry version 41.
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   ECO:0000313|EMBL:EGS32153.1};
GN   ORFNames=HMPREF1040_0472 {ECO:0000313|EMBL:EGS32153.1};
OS   Megasphaera sp. UPII 135-E.
OC   Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=1000569 {ECO:0000313|EMBL:EGS32153.1, ECO:0000313|Proteomes:UP000004137};
RN   [1] {ECO:0000313|EMBL:EGS32153.1, ECO:0000313|Proteomes:UP000004137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UPII 135-E {ECO:0000313|EMBL:EGS32153.1,
RC   ECO:0000313|Proteomes:UP000004137};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B.,
RA   Sutton G.G., Nelson K.E.;
RL   Submitted (JUN-2011) 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:SAAS00731907}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00756131}.
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:EGS32153.1}.
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DR   EMBL; AFUG01000043; EGS32153.1; -; Genomic_DNA.
DR   RefSeq; WP_007393177.1; NZ_AFUG01000043.1.
DR   STRING; 1000569.HMPREF1040_0472; -.
DR   EnsemblBacteria; EGS32153; EGS32153; HMPREF1040_0472.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000004137; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
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:SF12; PTHR30050:SF12; 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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000004137};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004137}.
FT   DOMAIN      188    318       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      403    472       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     196    203       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   498 AA;  56908 MW;  25413AEC8A2F8144 CRC64;
     MTELDVTTLW IGMLNKLKET IPPNLYTIWI ESSIIPYSYE NNILILDTSQ KFLCSYLSNN
     YLDDLKKAAF SVTGVPTTVK LICSAKESPD TTTPSKTVDK SDLQPIPKQV KETHTDFELV
     PVNMTLSTSE KKKETPSLSI KEAKNISIPS TENQLDTTYT FDSFIVGNSN RIAFAKALAV
     AEAPGRKEFN PLYIYGASGL GKTHLMHAIG HSILKKFPHM RLRSITSEDF VNEFIKCIQD
     KNTESFRQQY RNIDVLLVDD IQFLGRGDKD SSKEEFFHTF NKLQQDKKQI VLTSDRPPLD
     IERMEERLRS RFQSGSVAWI DPPDLETRTA ILKTWADKYN LSIDNDAINY IASNVSENIR
     ELSGAFNNIR DLASTEHTSI TLSLTQRALR YLIQNKTTKK YISIEEIINV VCKFYNINYK
     DIMGKKKTKD IALPRQIAMY LCRELTENTY PYIGTCFGGR DHTTVMHACT KINTKYIADE
     RFKNSIDKLI NTIKQVDN
//
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