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Database: UniProt
Entry: Q1NPZ0_9DELT
LinkDB: Q1NPZ0_9DELT
Original site: Q1NPZ0_9DELT 
ID   Q1NPZ0_9DELT            Unreviewed;       447 AA.
AC   Q1NPZ0;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   25-OCT-2017, entry version 71.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=MldDRAFT_3886 {ECO:0000313|EMBL:EAT03778.1};
OS   delta proteobacterium MLMS-1.
OC   Bacteria; Proteobacteria; Deltaproteobacteria.
OX   NCBI_TaxID=262489 {ECO:0000313|EMBL:EAT03778.1, ECO:0000313|Proteomes:UP000005853};
RN   [1] {ECO:0000313|EMBL:EAT03778.1, ECO:0000313|Proteomes:UP000005853}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MLMS-1 {ECO:0000313|EMBL:EAT03778.1,
RC   ECO:0000313|Proteomes:UP000005853};
RG   US DOE Joint Genome Institute (JGI-ORNL);
RA   Larimer F., Land M., Hauser L.;
RT   "Annotation of the draft genome assembly of delta proteobacterium
RT   MLMS-1.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EAT03778.1, ECO:0000313|Proteomes:UP000005853}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MLMS-1 {ECO:0000313|EMBL:EAT03778.1,
RC   ECO:0000313|Proteomes:UP000005853};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Bruce D.,
RA   Pitluck S., Richardson P.;
RT   "Sequencing of the draft genome and assembly of delta proteobacterium
RT   MLMS-1.";
RL   Submitted (APR-2006) 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:SAAS00724167}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00911680}.
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:EAT03778.1}.
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DR   EMBL; AAQF01000103; EAT03778.1; -; Genomic_DNA.
DR   RefSeq; WP_007293566.1; NZ_AAQF01000103.1.
DR   ProteinModelPortal; Q1NPZ0; -.
DR   EnsemblBacteria; EAT03778; EAT03778; MldDRAFT_3886.
DR   PATRIC; fig|262489.9.peg.3177; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000005853; 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; 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; IPR024633; DnaA_N_dom.
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   Pfam; PF11638; DnaA_N; 1.
DR   PRINTS; PR00051; DNAA.
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   Complete proteome {ECO:0000313|Proteomes:UP000005853};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
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:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005853}.
FT   DOMAIN      352    420       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     148    155       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   447 AA;  50112 MW;  E9A4EBD345D31910 CRC64;
     MIWPEVRKIL QKRLPESVFN LWIEPLSCLE EGDGRLELAG PDRFFCNWVA ENHLTDIQAA
     LKEMDREGLA VRFQVDRQAG ASEEEAGEGA EQLRLPRMPR NHNRVRTLHP RYTFDEFMVG
     DSNALAHSAC EAIATGTTQA EPCVFINAGT GLGKSHLTHA VAHHLYNNAP GTRLCCLTSQ
     QLTAELVHHI RNNSMEQFKE KFQRRCDVLL VEDVQTLSGR SKTQVELAEA VDSLLDSGRR
     VLFTGSRSPR EIPDLDEGVR SRLASGLVTT INPPDIKTRR LIIRRKAVFH KLALDEEMVA
     YIAEKVRGDI RKVESAIVGL KAKANLRRIA PTTEMVREVV ATVAGEEAPG LNSEAIRDFV
     AAQFKLSVEE LRSKSRKKEI TFPRQVSMYL ARKLTDEGLA GIGKAFDRDH STVVHSIRVI
     NEAVARNGSV RGQIEHLTKR LRQRDQG
//
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