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Database: UniProt
Entry: F9ED39_9ACTO
LinkDB: F9ED39_9ACTO
Original site: F9ED39_9ACTO 
ID   F9ED39_9ACTO            Unreviewed;       531 AA.
AC   F9ED39;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   25-OCT-2017, entry version 42.
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:EGQ75556.1};
GN   ORFNames=HMPREF9062_0361 {ECO:0000313|EMBL:EGQ75556.1};
OS   Actinomyces sp. oral taxon 448 str. F0400.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=888056 {ECO:0000313|EMBL:EGQ75556.1, ECO:0000313|Proteomes:UP000005351};
RN   [1] {ECO:0000313|EMBL:EGQ75556.1, ECO:0000313|Proteomes:UP000005351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0400 {ECO:0000313|EMBL:EGQ75556.1,
RC   ECO:0000313|Proteomes:UP000005351};
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 (MAY-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:SAAS00735475}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00911680}.
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:EGQ75556.1}.
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DR   EMBL; AFQC01000013; EGQ75556.1; -; Genomic_DNA.
DR   RefSeq; WP_009748264.1; NZ_GL985606.1.
DR   STRING; 888056.HMPREF9062_0361; -.
DR   EnsemblBacteria; EGQ75556; EGQ75556; HMPREF9062_0361.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000005351; 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; 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   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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005351};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005351}.
FT   DOMAIN      221    355       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      433    502       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     229    236       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   531 AA;  58277 MW;  0942E21B74B1DCD1 CRC64;
     MPDDTTTRWQ SVLEVLAESA ELSTGKLSII RMTRVIDVDG TLVLVAGSPF TKSKVEEART
     AISRALAQVW GREIPFEVTV DTSLEAGAPI PTISSSRPPA QPAPDQSSSF ASTSGPIARS
     EPVTPAEPVV RARPHIAEAS MSTTADGSTS MQSTTPTYVT NPAAAFARPE SPQTFDKSSR
     LNPRYSFDNY VMGDSNRFAF AAALKVAEQP GDADPDRSTG GYNPLFIYGG SGLGKTHLLH
     AIGNHARSLY RDMIIKYVSS EEFVSDFIAS VAEGKMNDFK RRYRDVDILL VDDVQFLGGK
     EQTLEEFFHT FNTLYMANKQ VVLTSDLPPK DLRGFEKRLL SRFESGLTVD VQPPTLETRT
     AILRNKARAE GVDLPMPVLE YIAGRVTTNI RELEGALIRV TAFASLTDQP IDQTLAEMVL
     KDIISNSGGG EITAAMVMTQ TADFFGLTIE DLRSKDRAQT MVHARHIAMY LCRELIEMST
     TKIGKEFGGK DHTTVMSASR KISTQMAERR DTYNQVQEIT ARIKQASQAP R
//
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