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Database: UniProt
Entry: L8TPV6_9MICC
LinkDB: L8TPV6_9MICC
Original site: L8TPV6_9MICC 
ID   L8TPV6_9MICC            Unreviewed;       473 AA.
AC   L8TPV6;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   28-MAR-2018, entry version 39.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01020005};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:ELT45318.1};
GN   ORFNames=G205_06468 {ECO:0000313|EMBL:ELT45318.1};
OS   Arthrobacter nitrophenolicus.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=683150 {ECO:0000313|EMBL:ELT45318.1, ECO:0000313|Proteomes:UP000011189};
RN   [1] {ECO:0000313|EMBL:ELT45318.1, ECO:0000313|Proteomes:UP000011189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJCon {ECO:0000313|EMBL:ELT45318.1,
RC   ECO:0000313|Proteomes:UP000011189};
RA   Vikram S., Kumar S., Vaidya B., Pinnaka A.K., Raghava G.P.S.;
RT   "Draft Genome Sequence of the 2-Chloro-4-Nitrophenol-Degrading
RT   Bacterium Arthrobacter sp. Strain SJCon.";
RL   Genome Announc. 1:E00058-13(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}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00747961}.
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:ELT45318.1}.
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DR   EMBL; AOFD01000010; ELT45318.1; -; Genomic_DNA.
DR   RefSeq; WP_009357110.1; NZ_AOFD01000010.1.
DR   EnsemblBacteria; ELT45318; ELT45318; G205_06468.
DR   PATRIC; fig|683150.5.peg.1294; -.
DR   Proteomes; UP000011189; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
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:SF2; PTHR30050:SF2; 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:SAAS00747950};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000011189};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00747973};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00748008};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011189}.
FT   DOMAIN      164    292       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      376    445       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     172    179       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      445    465       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   473 AA;  53218 MW;  62275D66084F19F7 CRC64;
     MTVDEANHAN TVGSSWRRVV SLLEQDHRVS PRQRGFVILA QAQGLIGSTL LVAVPNELTR
     EVLQTQVKDA LDDALHSVFS EDIRCAIDVD TDLVPVHEEP EPVVEPSFVS DQLVEQKPQP
     MLPSTSHEFG RLNPKYVFDT FVIGSSNRFA HAAAVAVAEA PAKAYNPLFI YGDSGLGKTH
     LLHAIGHYAR RLYSGIRVRY VNSEEFTNDF INSIRDDEGA SFKTTYRNVD VLLIDDIQFL
     AGKDRTLEEF FHTFNSLHNN NKQVVITSDQ PPKLLAGFED RMKSRFEWGL LTDIQPPELE
     TRIAILRKKA LSEGLSAPDD ALEYIASKIS SNIRELEGAL IRVTAFASLN RQPVDVALAE
     MVLKDLITDD GAQEITSSQI LQQTADYFKL SMEELCSKSR TRTLVTARQI AMYLCRELTD
     MSLPKIGQEL GGRDHTTVIH ADRKIRELMA ERRVIYNQVT ELTNRIKQQQ RDS
//
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