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Database: UniProt
Entry: U2PIJ1_9ACTN
LinkDB: U2PIJ1_9ACTN
Original site: U2PIJ1_9ACTN 
ID   U2PIJ1_9ACTN            Unreviewed;       488 AA.
AC   U2PIJ1;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-SEP-2017, entry version 31.
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:ERK50380.1};
GN   ORFNames=HMPREF0682_1423 {ECO:0000313|EMBL:ERK50380.1};
OS   Propionibacterium acidifaciens F0233.
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Propionibacterium.
OX   NCBI_TaxID=553198 {ECO:0000313|EMBL:ERK50380.1, ECO:0000313|Proteomes:UP000017052};
RN   [1] {ECO:0000313|EMBL:ERK50380.1, ECO:0000313|Proteomes:UP000017052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0233 {ECO:0000313|EMBL:ERK50380.1,
RC   ECO:0000313|Proteomes:UP000017052};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M.,
RA   Haft D.H., Methe B., Sutton G., Nelson K.E.;
RL   Submitted (AUG-2013) 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:ERK50380.1}.
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DR   EMBL; ACVN02000307; ERK50380.1; -; Genomic_DNA.
DR   RefSeq; WP_021798757.1; NZ_ACVN02000307.1.
DR   EnsemblBacteria; ERK50380; ERK50380; HMPREF0682_1423.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000017052; 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: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.
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:UP000017052};
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:UP000017052}.
FT   DOMAIN      178    307       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      391    460       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     186    193       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   488 AA;  54570 MW;  9708E46DD1E09E02 CRC64;
     MATEPGTSRN EPDFTRAWEH VLSECGTSGG AFLRNAKPLT VHESTMMVAV PNDFTRERIE
     TKMRGALEEA LSDYYRRSMH LALTIEPDLE LDLRAPDHDD EGTGEARREE SAPRFVPRKG
     APSLLLSESA GPSSSAPDPN GSEQRLNPRY TFDNFVIGAS NRFAHAAAVA VAEAPGKAYN
     PLMIYGESGL GKTHLLHALG HYVIDYYEGV RVKYVSTEEM TNEFINAVGE NRTVEFRRKY
     RDDVDVLLVD DIQFLEGKTQ TQEEFFYTFN ALHNAQKQIV LTSDRPPKAL EQLESRLRSR
     FEWGLITDIQ PPDLETRIAI LQRKALAEQL LVPADVLEFI GSRIQTNIRE LEGALIRVTA
     FASLNREPVT HDLADRVLAD LIPDGTDAEV SAQLIIAETA GYFDVSVEAL SGSSRTQPLV
     LARQIAMYLC RELTDLSLPK IGQEFGGKDH TTVMHADRKI RELMRKQRSV FNQVSELTNR
     IKQAAARG
//
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