GenomeNet

Database: UniProt
Entry: A0A117M9E7_9BACT
LinkDB: A0A117M9E7_9BACT
Original site: A0A117M9E7_9BACT 
ID   A0A117M9E7_9BACT        Unreviewed;       473 AA.
AC   A0A117M9E7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   25-OCT-2017, entry version 13.
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=XE04_0909 {ECO:0000313|EMBL:KUK91691.1};
OS   Marinimicrobia bacterium 46_43.
OC   Bacteria; Candidatus Marinimicrobia.
OX   NCBI_TaxID=1635280 {ECO:0000313|EMBL:KUK91691.1, ECO:0000313|Proteomes:UP000054945};
RN   [1] {ECO:0000313|EMBL:KUK91691.1, ECO:0000313|Proteomes:UP000054945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=46_43 {ECO:0000313|EMBL:KUK91691.1};
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-resolved metagenomic analysis reveals roles for candidate
RT   phyla and other microbial community members in biogeochemical
RT   transformations in oil reservoirs.";
RL   MBio 7:e01669-15(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: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:KUK91691.1}.
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; LGGY01000130; KUK91691.1; -; Genomic_DNA.
DR   PATRIC; fig|1635280.3.peg.844; -.
DR   Proteomes; UP000054945; 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; 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; 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   Complete proteome {ECO:0000313|Proteomes:UP000054945};
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:UP000054945}.
FT   DOMAIN      166    300       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      378    447       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     174    181       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   473 AA;  54048 MW;  381D0E46EC0E4A0F CRC64;
     MAIVDKMDSE MLKKWDALLE DLQKYIPTHS YTSWFLPLQP VSSNEQALRI SAPNRFHSEY
     VEMHYRDVLR KCIKSVFGKD LIVQFTIAES LKKDISSGNS TPESPLPPPV TERGDRENLP
     PQEYYVEDRY SQLNGRYTFE TFVEGPHNQF AKVASRAVAE APGNTAFNPL LIYGGTGLGK
     THLLQAIGHY ARTRNPNRRV IYVSSEKFMV DFITAIRNNR LNEFGNIYRK ADLLLVDDIQ
     FLESREGTQE QFFHTFNDLY QHGKQIVITS DRTPKELKGV EERLISRFLS GLTVDIQPPD
     FESRIAILQK KADMDQVIIP PEVIEFVAQN ITTNVRELEG AMTRIFAYSS LAHTDVTINL
     AKKVIKDILG VRKARHISID IIQSAVSDYY KVTENELMGK GRKREVALAR QVIMFLSREI
     SGMSLKTIGL RLGRRDHTTV MHACNVIGKK IRENKEFARE IDTIRHQIDL TAG
//
DBGET integrated database retrieval system