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Database: UniProt
Entry: E0QN54_9ACTO
LinkDB: E0QN54_9ACTO
Original site: E0QN54_9ACTO 
ID   E0QN54_9ACTO            Unreviewed;       533 AA.
AC   E0QN54;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, 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:EFM47006.1};
GN   ORFNames=HMPREF0580_0318 {ECO:0000313|EMBL:EFM47006.1};
OS   Mobiluncus mulieris ATCC 35239.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae;
OC   Mobiluncus.
OX   NCBI_TaxID=871571 {ECO:0000313|EMBL:EFM47006.1, ECO:0000313|Proteomes:UP000003045};
RN   [1] {ECO:0000313|EMBL:EFM47006.1, ECO:0000313|Proteomes:UP000003045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35239 {ECO:0000313|EMBL:EFM47006.1,
RC   ECO:0000313|Proteomes:UP000003045};
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 (AUG-2010) 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:EFM47006.1}.
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DR   EMBL; AEET01000011; EFM47006.1; -; Genomic_DNA.
DR   RefSeq; WP_004013503.1; NZ_GL405260.1.
DR   EnsemblBacteria; EFM47006; EFM47006; HMPREF0580_0318.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000003045; 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; 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:UP000003045};
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:UP000003045}.
FT   DOMAIN      222    350       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      436    505       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     230    237       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   533 AA;  58568 MW;  0986B9E6779EA5A3 CRC64;
     MPSFRQIFSR RSERCVNLVA SGTSTSYEAG DFLSPALDEL RESGKISDFD LVLLRQSKAL
     AHNEDAAVLA VPGTMVKGII DAKYTPDLKA AFSKILGKTI NNLVITVDEG LVKQNSATTP
     GATPKNIGIT SPLTSPNGMA PRENNPNLEN PNPNPSLTTP NTTPTGNLAN PATIPAPIPA
     SMQIDRNTGL NPMYTFESFV IGSSNSFTAA AAESVVVSPA QAYNPLFIYG GSGLGKTHLL
     HAIGNYALEL YPQAKVRYVS SEEFTNDFIN AIATQTFPEL QAKYREVDFL LIDDIQFLQG
     KEQTLEEFFH TFNTLHTARK QVVITSDVPP KELKSFEERI KSRLEWGLLT DIQPPNLETR
     IAILRRKSAQ ENLQGYDDAV LEYIASNISS NIRELEGALL RVTAYAALSG GGSVSLDTAK
     EILRDFITGR NTRDITPQMI IEQTAQYFGL EVDEIMSTDR SRTVVNSRQV AMYLCRELTE
     LSLPKVGEAF GGRDHTTVMH AVKKIEKTIN EDSQTYQSIT EITNQIRRAA VRG
//
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