GenomeNet

Database: UniProt
Entry: S6GNF8_9GAMM
LinkDB: S6GNF8_9GAMM
Original site: S6GNF8_9GAMM 
ID   S6GNF8_9GAMM            Unreviewed;       494 AA.
AC   S6GNF8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   05-JUL-2017, entry version 31.
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=OFPI_30980 {ECO:0000313|EMBL:EPJ48053.1};
OS   Osedax symbiont Rs2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   unclassified Oceanospirillaceae.
OX   NCBI_TaxID=1330035 {ECO:0000313|EMBL:EPJ48053.1, ECO:0000313|Proteomes:UP000014830};
RN   [1] {ECO:0000313|EMBL:EPJ48053.1, ECO:0000313|Proteomes:UP000014830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rs2 {ECO:0000313|Proteomes:UP000014830};
RA   Yi H., Goffredi S.;
RT   "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT   Osedax worms: functional variation and environmental selection.";
RL   Submitted (MAY-2013) 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: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:EPJ48053.1}.
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; ASZI01000243; EPJ48053.1; -; Genomic_DNA.
DR   PATRIC; fig|1330035.3.peg.2986; -.
DR   Proteomes; UP000014830; 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; IPR024633; DnaA_N_dom.
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   Pfam; PF11638; DnaA_N; 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:UP000014830};
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:UP000014830}.
FT   DOMAIN      191    396       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      402    471       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     199    206       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   494 AA;  55376 MW;  1EECA8D366C631DB CRC64;
     MSIELWDRCL QSLQNEFPSQ QYNTWIRPLQ AEATDTALIL IAPNRFVRDW VNDKFLSRIT
     QVVCDVANDA GLVVRIEVRQ AAGAAPLSMP VVQPRIRPSP RVSVNQNIER EHNDPVPVPA
     PVARNYNEPA PQLELDVGNY GRSSRVVDVE GGLRHQSNLN EAFTFNSFVG GKSNQLALAA
     AQQVSDNPGG SYNPLFIYGG VGLGKTHLMH AVGMELLKKN PSARIVYLHS ERFVADMVKA
     LQLNAINDFK RYYRSVDALL IDDIQFFAGK ERSQEEFFHT FNALLEGGQQ MILTSDRYPK
     EIAGVEDRLK SRFGWGLTVA VEPPELETRV AIVMKKAQEA GVMLPDDAAF FLAQKIRSNV
     RELEGALKRV IANAHFTGNA ITTAFIKESL KDLLALQDKQ VSIDNIQRVV AEYYKIKIAD
     LLSKRRNRSV ARPRQVAMSL AKELTNHSLP EIGDAFGGRD HTTVLHACRK IKELRESDAD
     IREDYQNLLR HLTA
//
DBGET integrated database retrieval system