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Database: UniProt
Entry: A0A124IH27_9SPHN
LinkDB: A0A124IH27_9SPHN
Original site: A0A124IH27_9SPHN 
ID   A0A124IH27_9SPHN        Unreviewed;       488 AA.
AC   A0A124IH27;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   05-JUL-2017, entry version 10.
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=APF82_03350 {ECO:0000313|EMBL:KUO52010.1};
OS   Sphingomonadales bacterium BRH_c42.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   unclassified Sphingomonadales.
OX   NCBI_TaxID=1734407 {ECO:0000313|EMBL:KUO52010.1, ECO:0000313|Proteomes:UP000054281};
RN   [1] {ECO:0000313|EMBL:KUO52010.1, ECO:0000313|Proteomes:UP000054281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c42 {ECO:0000313|EMBL:KUO52010.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) 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:KUO52010.1}.
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DR   EMBL; LOEX01000119; KUO52010.1; -; Genomic_DNA.
DR   Proteomes; UP000054281; 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:UP000054281};
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:UP000054281}.
FT   DOMAIN      184    312       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      396    465       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     192    199       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   488 AA;  54830 MW;  373FB09FED6CCB00 CRC64;
     MVQNQENAQI SKRKRDEDLM EDAEAVNLAA DWADISQGLR KDLGHQLHSQ WIRPIQLGSF
     CKDSGTLDLF LPTEFSANWV NDRFHDRLQL AWKIARSEVR KVRIQVHPGR RKLPELRLEN
     GRHPANDGLD NRSFAVGAGA MGDAGFSSSV GLDPSLTFAA FVTGEANVLA CNAAQRMAAT
     EQPQFSPLYL KAATGQGKTH LLHAIGHAYL AAHTRARIFY CSAERFMVEF VQALKANQMI
     EFKARLRSFD LLLVDDIQFI IGKASAQEEL LYTIDALLAE GKRLVFAADR APQALDGVEP
     RLLSRLSMGL VADIQPADIE LRRSILESKL TRFAPLEVPG DVLEFLARTI TRNVRELVGG
     LNKLIAYAQL TGQEVSLQLA EEQLTDILSA NRRRITIDEI QRTVCQFYRI DRAEMSSKRR
     ARAVVRPRQV AMYLAKVLTP RSYPEIGRKF GGRDHSTVIH AVRLIEDLRQ RDADMDGDVR
     SLLRQLES
//
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