GenomeNet

Database: UniProt
Entry: A0A0P0SJ45_9PSEU
LinkDB: A0A0P0SJ45_9PSEU
Original site: A0A0P0SJ45_9PSEU 
ID   A0A0P0SJ45_9PSEU        Unreviewed;       570 AA.
AC   A0A0P0SJ45;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   05-JUL-2017, entry version 16.
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=AD017_13375 {ECO:0000313|EMBL:ALL84607.1};
OS   Pseudonocardia sp. EC080619-01.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Pseudonocardia.
OX   NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL84607.1, ECO:0000313|Proteomes:UP000066228};
RN   [1] {ECO:0000313|EMBL:ALL84607.1, ECO:0000313|Proteomes:UP000066228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL84607.1,
RC   ECO:0000313|Proteomes:UP000066228};
RX   PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA   Van Arnam E.B., Sit C.S.;
RT   "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL   J. Am. Chem. Soc. 137:14272-14274(2015).
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; CP012184; ALL84607.1; -; Genomic_DNA.
DR   RefSeq; WP_029239553.1; NZ_CP012184.1.
DR   EnsemblBacteria; ALL84607; ALL84607; AD017_13375.
DR   KEGG; pecq:AD017_13375; -.
DR   PATRIC; fig|1096856.3.peg.2800; -.
DR   KO; K02313; -.
DR   Proteomes; UP000066228; 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:UP000066228};
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:UP000066228}.
FT   DOMAIN      262    390       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      474    543       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     270    277       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   570 AA;  61587 MW;  F79A72FEC369D739 CRC64;
     MTDQPGDLGA VWNRVIADLS GSSADSGTPA LSPQQRAFLR LTRPLGLLDG TALLAAPSEF
     AKDAIERILR RPISDALGRH LGVSVNLAVV VDASAASGGT EVPDPPGFGL PRGVTAGDSA
     RDTGTPEAAA SAALSEGSDD TSGTVALDDG TEPATGTGDD GPGTAADDLP AADTGRSRAY
     PSETTVSSGG WAPQPPSADS GSRDGGGTSW PAYTAPQAGD PVAPRSQTRL NERYTFDTFV
     IGASNRFSHA AAVAVSEAPA RAYNPLFIWG ESGLGKTHLL HAVGHYAQRL FPGMRVRYVS
     TEEFTNDFIN SLRDDRKVAF QRRYRDVDVL LVDDIQFLEG KEGTQEEFFH TFNTLHNANK
     QIVVSSDRPP KRLETLEDRM RTRFEWGLIT DIQPPELETR IAILRKKAAQ DRLAVPGEVL
     EFIAERIERN IRELEGALIR VTAFASLNRQ AVDTQLAEIV LRDLIPDSAA SEITAPTIMA
     VTAEFFGVTL DDLSGPGKTK ALAQARQIAM YLCRELTDLS LPRIGQTFGG RDHTTVMHAD
     KKIRNEISLR RKTFEQVQEL TARIKLRARH
//
DBGET integrated database retrieval system