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Database: UniProt
Entry: A0A0F2TBZ1_9ACTN
LinkDB: A0A0F2TBZ1_9ACTN
Original site: A0A0F2TBZ1_9ACTN 
ID   A0A0F2TBZ1_9ACTN        Unreviewed;       606 AA.
AC   A0A0F2TBZ1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   05-JUL-2017, entry version 18.
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=VM95_19935 {ECO:0000313|EMBL:KJS60679.1};
OS   Streptomyces rubellomurinus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=359131 {ECO:0000313|EMBL:KJS60679.1, ECO:0000313|Proteomes:UP000033699};
RN   [1] {ECO:0000313|EMBL:KJS60679.1, ECO:0000313|Proteomes:UP000033699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31215 {ECO:0000313|EMBL:KJS60679.1,
RC   ECO:0000313|Proteomes:UP000033699};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-2015) 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:KJS60679.1}.
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DR   EMBL; JZKH01000039; KJS60679.1; -; Genomic_DNA.
DR   RefSeq; WP_045698685.1; NZ_JZKH01000039.1.
DR   EnsemblBacteria; KJS60679; KJS60679; VM95_19935.
DR   PATRIC; fig|359131.3.peg.4649; -.
DR   Proteomes; UP000033699; 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; 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:UP000033699};
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:UP000033699}.
FT   DOMAIN      299    427       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      514    583       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     307    314       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   606 AA;  66827 MW;  89CC26D3742B0563 CRC64;
     MADVNSDLVP VWARVVERLV NDPDVGEMDK QWVQRTQPMW MMHDTALLAT PNERAKQVLE
     GRLLPQLTEA LSRELSRPVR IAVMVDANAV PSTPAPAPQP PVEPYPGPAE EGTGGYGGQG
     YQQPYEPDYE QPQDYERPRY DTGGYEQRPA PYGGQPGPQS WPGYQEQQAP YRDHEEAAPR
     QAPRPVPSPP STTQGDLFGG AYGPGPNEQP RAGAGRRSPG SRPTGGRPAE KAPAERAPER
     PGVPGVPAPP GAPPAGGSRK DEPAARLNPK YLFDTFVIGA SNRFAHAAAV AVAEAPAKAY
     NPLFIYGESG LGKTHLLHAI GHYSRSLFPG TRVRYVSSEE FTNEFINSIR DGKADTFRRR
     YRDMDILLVD DVQFLASKES TQEEFFHTFN TLHNANKQIV LSSDRPPKLL TTLEDRLRNR
     FEWGLITDVT PPELETRIAI LRKKAIQEQL NAPADVLEFI ASRITRNIRE LEGALIRVTA
     FANLNRAPVD LELAGIVLKD LIPGGDEDAG PEITAQVIMQ QTAAYFGLGV DDLCGSSRSR
     VLVTARQIAM YLCRELTDLS LPKIGAQFGG RDHTTVMHAD RKIRSLMAER RSIYNQVTEL
     TNRIKS
//
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