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Database: UniProt
Entry: A0A095XLR9_9FIRM
LinkDB: A0A095XLR9_9FIRM
Original site: A0A095XLR9_9FIRM 
ID   A0A095XLR9_9FIRM        Unreviewed;       445 AA.
AC   A0A095XLR9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-SEP-2017, entry version 25.
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=HMPREF1633_07450 {ECO:0000313|EMBL:KGF11065.1};
OS   Tissierellia bacterium S5-A11.
OC   Bacteria; Firmicutes; Tissierellia.
OX   NCBI_TaxID=1230730 {ECO:0000313|EMBL:KGF11065.1, ECO:0000313|Proteomes:UP000029576};
RN   [1] {ECO:0000313|EMBL:KGF11065.1, ECO:0000313|Proteomes:UP000029576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S5-A11 {ECO:0000313|EMBL:KGF11065.1,
RC   ECO:0000313|Proteomes:UP000029576};
RA   McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JUL-2014) 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: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:KGF11065.1}.
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DR   EMBL; JRMZ01000020; KGF11065.1; -; Genomic_DNA.
DR   RefSeq; WP_034438137.1; NZ_JRMZ01000020.1.
DR   EnsemblBacteria; KGF11065; KGF11065; HMPREF1633_07450.
DR   Proteomes; UP000029576; 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:SF12; PTHR30050:SF12; 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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029576};
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:UP000029576}.
FT   DOMAIN      139    273       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      351    420       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     147    154       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   445 AA;  50955 MW;  25CB68D9B2242906 CRC64;
     MDQDLLHLWG NFLSELQKTE ISPITYDTFF KQLSPIKLEN DTLFINTPTS FIGEHICNNE
     SYHRYMVDIF NRLTEKNLNF KFLVGDAPYN SFQTSSQDQL YERSRLNPKY TFDTFVVGKS
     NEFAHAASVS VADSLEKANA NPLFIYGGVG LGKTHLMHAI GHFVLDRDPK KKVLYVTSEQ
     FTNEFINSIR TNKNEHFRHK YRSMDLLLID DIQFIADKET TMEEFFHTFN ELYAADKQIV
     LTSDKPPNTI PKLESRLISR FAGGLVVDIA PPDLETRIAI LRKKSDAEGF QVPDDVINFI
     AEQVQSNIRE LEGALSRVTA YSRLTTGTIS IKTASLALKD LYREQTTKPI TPEAIKKVIS
     RHYNVSLEDL DSKKRTRSIA YPRQIAMYMS RQYTDLSLLK IGETFGGRDH STVIHAYEKV
     SEDVENNPSL NAKIHQMIRE VKGEL
//
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