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Database: UniProt
Entry: A0A095YY05_9ACTO
LinkDB: A0A095YY05_9ACTO
Original site: A0A095YY05_9ACTO 
ID   A0A095YY05_9ACTO        Unreviewed;       484 AA.
AC   A0A095YY05;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   25-OCT-2017, entry version 27.
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   ORFNames=HMPREF1627_03295 {ECO:0000313|EMBL:KGF01139.1};
OS   Actinomyces sp. S6-Spd3.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=1284680 {ECO:0000313|EMBL:KGF01139.1, ECO:0000313|Proteomes:UP000029604};
RN   [1] {ECO:0000313|EMBL:KGF01139.1, ECO:0000313|Proteomes:UP000029604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S6-Spd3 {ECO:0000313|EMBL:KGF01139.1,
RC   ECO:0000313|Proteomes:UP000029604};
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: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:KGF01139.1}.
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DR   EMBL; JRMV01000272; KGF01139.1; -; Genomic_DNA.
DR   RefSeq; WP_034501014.1; NZ_JRMV01000272.1.
DR   EnsemblBacteria; KGF01139; KGF01139; HMPREF1627_03295.
DR   PATRIC; fig|1284680.3.peg.406; -.
DR   Proteomes; UP000029604; 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:UP000029604};
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:UP000029604}.
FT   DOMAIN      172    299       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      383    452       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     180    187       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   484 AA;  53441 MW;  914BA4DF2BB63627 CRC64;
     MSIDALTQAW SEALAQISDQ LRPATLSFLR SAKPLGDIDG TILIAVPNDF TKKWIENNDA
     TDLTASLTNI LGRSVRLAVT IDPSLEPEPE PVEQPSPVAS SVEGSDQVQP SATTPHQAAP
     AQATPSSSPQ LAIDTASTHL NPKHTFDTFV IGPSNRFAHA AAFAVSETPG RAYNPLFIHG
     DSGLGKTHLI HAIGHYTLSL FPQMRVRYVN SEEFTNDFIN SVREESIEEF QRRYREVDVL
     LIDDIQFIQG KERTVEEFFH TFNSLYNAGK QIVLTSDVPP RELDLEDRIR SRFAAGLLVD
     VLPPDLETRI AILQKKASAE NIEVDPRVLE YIAQRISSNI RELEGALVRV AAFESLSKEP
     VTVSMAEMLL KDFASDPQDT EVTPTLIMSQ TATYFGVTID QLSSSDRSHV VVEARQIAMY
     LCRELTDLSL PKIGAAFGGR DHTTVMHANK KIVGLMAEKR ETFNYVTELT NRIKQAARES
     ATLG
//
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