GenomeNet

Database: UniProt
Entry: H6N288_GORPV
LinkDB: H6N288_GORPV
Original site: H6N288_GORPV 
ID   H6N288_GORPV            Unreviewed;       556 AA.
AC   H6N288;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   05-JUL-2017, entry version 43.
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:AFA71080.1};
GN   OrderedLocusNames=GPOL_c00010 {ECO:0000313|EMBL:AFA71080.1};
OS   Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia.
OX   NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA71080.1, ECO:0000313|Proteomes:UP000009154};
RN   [1] {ECO:0000313|EMBL:AFA71080.1, ECO:0000313|Proteomes:UP000009154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX   PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA   Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D.,
RA   Angelov A., Liebl W., Daniel R., Steinbuchel A.;
RT   "Involvement of two latex-clearing proteins during rubber degradation
RT   and insights into the subsequent degradation pathway revealed by the
RT   genome sequence of Gordonia polyisoprenivorans strain VH2.";
RL   Appl. Environ. Microbiol. 78:2874-2887(2012).
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; CP003119; AFA71080.1; -; Genomic_DNA.
DR   RefSeq; WP_014358149.1; NC_016906.1.
DR   STRING; 1112204.GPOL_c00010; -.
DR   EnsemblBacteria; AFA71080; AFA71080; GPOL_c00010.
DR   KEGG; gpo:GPOL_c00010; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000009154; 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:UP000009154};
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:UP000009154}.
FT   DOMAIN      249    377       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      461    529       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     257    264       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   556 AA;  61046 MW;  D07ED74D3F2B346E CRC64;
     MTSDRDSFGE VWKQVVAELN DDAAHHEPLS RQQKAWLSLV QPLTLAEGFA LLAVPTPLVQ
     EQIERNLRDT IRTTLSRHLG QPVDLGVRTA TPAPLEETPD PATTDSVGSG ASTNPIPLSH
     TAFDESGPGR PIDPSAPGRP SPDGSGPLAG QGFAGREHRA PSDSFPHPTP SGAGYSGATD
     SSGPGAPNAT PGAEWSSYFA ERPTTSTASA SGTPVSLNPK YTFDTFVIGA SNRFAHASAV
     AVAEAPARAY NPLFIWGESG LGKTHLLHAA GHYAQRLFPG MRVKYVSTEE FTNDFINSLR
     DDRRVAFKRR YRDVDVLLVD DIQFLIGKEG IQEEFFHTFN TLHNTSKQIV ISSDRPPKQL
     ATLEDRLRTR FEWGLITDVQ PPDLETRIAI LRKKAQMDNI AVPDDVLELI ASKIERNIRE
     LEGALIRVTA FASLNNTELD KSLADVVLQA LLPNSGTIEI SAAGILAITA EYFDISVDEL
     RGPGKTRAIA QARQISMYLC RELTDLSLPK IGETFDRDHT TVMYAERKIR KEMAERRKVY
     DHVQELTARI KQRADR
//
DBGET integrated database retrieval system