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Database: UniProt
Entry: F2BWY5_9FIRM
LinkDB: F2BWY5_9FIRM
Original site: F2BWY5_9FIRM 
ID   F2BWY5_9FIRM            Unreviewed;       494 AA.
AC   F2BWY5;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-SEP-2017, entry version 39.
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:EGF14252.1};
GN   ORFNames=HMPREF9083_0703 {ECO:0000313|EMBL:EGF14252.1};
OS   Dialister micraerophilus DSM 19965.
OC   Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae;
OC   Dialister.
OX   NCBI_TaxID=888062 {ECO:0000313|EMBL:EGF14252.1, ECO:0000313|Proteomes:UP000003503};
RN   [1] {ECO:0000313|EMBL:EGF14252.1, ECO:0000313|Proteomes:UP000003503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19965 {ECO:0000313|EMBL:EGF14252.1,
RC   ECO:0000313|Proteomes:UP000003503};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z.,
RA   Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L.,
RA   Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D.,
RA   Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R.,
RA   San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S.,
RA   Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K.,
RA   Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (FEB-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:EGF14252.1}.
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DR   EMBL; AFBB01000012; EGF14252.1; -; Genomic_DNA.
DR   RefSeq; WP_007556010.1; NZ_GL878519.1.
DR   EnsemblBacteria; EGF14252; EGF14252; HMPREF9083_0703.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000003503; 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; 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.
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:UP000003503};
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:UP000003503}.
FT   DOMAIN      189    321       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      401    470       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     197    204       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   494 AA;  57600 MW;  6D98A1C9F8BBB287 CRC64;
     MNLFTLWGFI LEYIKKNDPQ YYEMFYKKIF PSLLDEKELT IITQDPYLVS WIEALYKTKL
     ETIISEKLNK PMKIIILSKE DHEEKKSEKI PDFMEEEKLP LMDEVKPYNP PENILINIPK
     NSQDIVLPSI QNYSKQTKIK EKPVYKSPNP INTEHTFETF VHGNCNEMAF QSALSVAQMA
     VNMEEMDKKM NPLFIYGPSG LGKTHLLHAI CNYIRENAPH LSYIFVSSET FTNELIASIK
     SNSMPKFREK YRNPDYLLID DVQFFGSKNS SKMEIFNTFN TLFDNKKHII LTSDRTPSDI
     EELEDRIQTR FSSGLIVPIS PPDYEICSII LEKRAEKEGI NIPSEVINYI AEHINTNVRE
     LDGAFNKLVT YAKVKKKEIT LEFAKETLKD QIPLEQNREI TPEIIINTVC NKFNVKKENL
     LGKGRPKNIV IPRQIAMYLC RKELNLSFPI LRDIFKRKDH STILYACERV EKDIAKDNET
     KKIIEELSNM LKNI
//
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