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Database: UniProt
Entry: A0A0L0K248_9ACTN
LinkDB: A0A0L0K248_9ACTN
Original site: A0A0L0K248_9ACTN 
ID   A0A0L0K248_9ACTN        Unreviewed;       644 AA.
AC   A0A0L0K248;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   05-JUL-2017, entry version 15.
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:KND31675.1};
GN   ORFNames=IQ63_25320 {ECO:0000313|EMBL:KND31675.1};
OS   Streptomyces acidiscabies.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=42234 {ECO:0000313|EMBL:KND31675.1, ECO:0000313|Proteomes:UP000037151};
RN   [1] {ECO:0000313|Proteomes:UP000037151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
RA   Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT   "Genome sequencing of plant-pathogenic Streptomyces species.";
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: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:KND31675.1}.
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DR   EMBL; JPPY01000145; KND31675.1; -; Genomic_DNA.
DR   EnsemblBacteria; KND31675; KND31675; IQ63_25320.
DR   PATRIC; fig|42234.21.peg.5236; -.
DR   Proteomes; UP000037151; 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:UP000037151};
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:UP000037151}.
FT   DOMAIN      337    465       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      551    620       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     345    352       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   644 AA;  71974 MW;  2B69210097483DE3 CRC64;
     MWPRVLEQLL GEGRGQGVEV KDERWLRRTQ PLALVADTAL LAVPNEFAKN VLEGRLAPIV
     SESLSRACGR PIRIAITVDE SAGEPPAPPQ PPYDEPEPPP QSYDKPPYDA PSRGDYEQQY
     DDPYDGGYGR HRPEPSGERP LPTVRPAYPG EYQRPEPGAW PRGAERPERS DEPGAWPRGE
     RSERGERPER SERSERAERA ERSDDYGGWQ QQRLGFPERD PYAGAPQEPY GQQEPYPSAP
     ERRPGGYRPA PAERGAYEPP SRPDYDQRDP VRRELPEPSH RPGGAPAPVS SAGGGKGPGE
     PTARLNPKYL FDTFVIGASN RFAHAAAVAV AEAPAKAYNP LFIYGESGLG KTHLLHAIGH
     YARSLYPGTR VRYVSSEEFT NEFINSIRDG KGDSFRKRYR EMDILLVDDI QFLADKESTQ
     EEFFHTFNTL HNANKQIVLS SDRPPKQLVT LEDRLRNRFE WGLITDVQPP ELETRIAILR
     KKAVQEQLNA PPEVLEFIAS RISRNIRELE GALIRVTAFA SLNRQPVDLG LTEIVLKDLI
     PGGEDSAPEI TSTAIMSATA AYFGLTVEDL CGTSRGRALV TARQIAMYLC RELTDLSLPK
     IGALFGGRDH TTVMHADRKI RNLMAERRSI YNQVTELTNR IKNG
//
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