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Database: UniProt
Entry: B1BC45_CLOBO
LinkDB: B1BC45_CLOBO
Original site: B1BC45_CLOBO 
ID   B1BC45_CLOBO            Unreviewed;       449 AA.
AC   B1BC45;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   30-AUG-2017, entry version 62.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:EDS76934.1};
GN   ORFNames=CBC_0994 {ECO:0000313|EMBL:EDS76934.1};
OS   Clostridium botulinum C str. Eklund.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=445337 {ECO:0000313|EMBL:EDS76934.1, ECO:0000313|Proteomes:UP000003482};
RN   [1] {ECO:0000313|EMBL:EDS76934.1, ECO:0000313|Proteomes:UP000003482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund {ECO:0000313|EMBL:EDS76934.1,
RC   ECO:0000313|Proteomes:UP000003482};
RX   PubMed=23516187;
RA   Hassan K.A., Tetu S.G., Elbourne L.D., Johnson E.A., Paulsen I.T.;
RT   "Genome Sequence of the Group III Clostridium botulinum Strain Eklund-
RT   C.";
RL   Genome Announc. 1:E0004413-E0004413(2013).
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:SAAS00724167}.
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:EDS76934.1}.
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DR   EMBL; ABDQ01000011; EDS76934.1; -; Genomic_DNA.
DR   RefSeq; WP_003366904.1; NZ_ABDQ01000011.1.
DR   ProteinModelPortal; B1BC45; -.
DR   STRING; 445337.CBC_0994; -.
DR   EnsemblBacteria; EDS76934; EDS76934; CBC_0994.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000003482; 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; IPR018312; Chromosome_initiator_DnaA_CS.
DR   InterPro; IPR013317; DnaA.
DR   InterPro; IPR013159; DnaA_C.
DR   InterPro; IPR024633; DnaA_N_dom.
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   Pfam; PF11638; DnaA_N; 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:UP000003482};
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}.
FT   DOMAIN      144    272       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      356    425       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     152    159       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   449 AA;  51372 MW;  A2253C8AADA86E4B CRC64;
     MNAQLEQLWS KTLNIIKGEL TEVSFNTWIK SISPISITEN TIKLEVPNDF TRGILESRYK
     DLIINAIKLI TSKKYNIEFS ITSEEIFNNN QTNRTKSNNP NIVVNDEMTS ILNPKYTFDS
     FVIGNSNRFA HAASLAVAES PAKAYNPLFI YGGVGLGKTH LMHAIGHYIL QNTPNAKVVY
     VSSEKFTNEL INSIKDDKNE EFRNKYRNVD VLLIDDIQFI AGKERTQEEF FHTFNALYEA
     DKQIILSSDR PPKEIPTLED RLRSRFEWGL IADIQAPDFE TRIAILKKKA DVENLDIPNE
     VMVYIATKIK SNIRELEGAL IRIVAYSSLT NREISVDLAA EALKDIISSE QNKQVTIELI
     QDIVCNYFNL KIQELKSSRR TRNIAFPRQI AMYLSRKLTD MSLPKIGEEF GGRDHTTVIH
     AYEKISNILK KDESLRNVID DLNKKITNN
//
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