GenomeNet

Database: UniProt
Entry: U5VRE0_9ACTN
LinkDB: U5VRE0_9ACTN
Original site: U5VRE0_9ACTN 
ID   U5VRE0_9ACTN            Unreviewed;       626 AA.
AC   U5VRE0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   05-JUL-2017, entry version 32.
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=AFR_00005 {ECO:0000313|EMBL:AGZ38290.1};
OS   Actinoplanes friuliensis DSM 7358.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Actinoplanes.
OX   NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ38290.1, ECO:0000313|Proteomes:UP000017746};
RN   [1] {ECO:0000313|EMBL:AGZ38290.1, ECO:0000313|Proteomes:UP000017746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ38290.1,
RC   ECO:0000313|Proteomes:UP000017746};
RX   PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA   Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA   Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT   "Complete genome sequence of the actinobacterium Actinoplanes
RT   friuliensis HAG 010964, producer of the lipopeptide antibiotic
RT   friulimycin.";
RL   J. Biotechnol. 178:41-42(2014).
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP006272; AGZ38290.1; -; Genomic_DNA.
DR   RefSeq; WP_023357234.1; NC_022657.1.
DR   EnsemblBacteria; AGZ38290; AGZ38290; AFR_00005.
DR   KEGG; afs:AFR_00005; -.
DR   PATRIC; fig|1246995.3.peg.1; -.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000017746; Chromosome.
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; 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:UP000017746};
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:UP000017746}.
FT   DOMAIN      320    448       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      532    601       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     328    335       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   626 AA;  70191 MW;  FD831411980ED4A9 CRC64;
     MADTVDLGGV WTAATDELAD EIASAQQRAY LRLTRLRAIV EDTALLSVPD TYTRDVIESR
     LRLAITEALS RRLGRPIQVA VTVRPPEDGS GRPGTVYGTP PPEPPTQPPA HYADQQQHQQ
     PAYQDHYQQG PSFGHPQTFD DQYENEGPTG SAQAPFARPV PVARDGQDAL FAAPMPQQQP
     DSKSSAPEQK EVATRTDAEP QRREAPRQMS HFADPSNDPG GHRMAGDQSQ LRDNQRRPDD
     RPPMHGQDRR DDTLQMRHGG DNGPGRAPMD MRGQSGDRRP GGNDGNRLNP KYMFETFVIG
     SSNRFAHAAS VAVAESPAKA YNPLFIYGSS GLGKTHLLHA IGHYATTLGH ARSVRYVSTE
     EFTNDFINSL RDDKTQAFQR RYRDVDILLI DDIQFLENRE RTQEEFFHTF NTLHNANKQI
     VISSDRSPRQ LATLEDRMRT RFEWGLLADI QPPDLETRIA ILQKKAAQER MYAPDDVLEF
     IASRVSNSIR ELEGALIRVT AFASLTRSSV QLSLAEEVLR DFMPDGAGPE ITADQIMVST
     ADYFGVSLED LRGHSRSRVL VNARQVAMYL CRELTELSLP RIGQAFGGRD HTTVMHADRK
     IRQHMAERRS LYNQIAELTN RIKQNT
//
DBGET integrated database retrieval system