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Database: UniProt
Entry: I2K5K3_9PROT
LinkDB: I2K5K3_9PROT
Original site: I2K5K3_9PROT 
ID   I2K5K3_9PROT            Unreviewed;       444 AA.
AC   I2K5K3;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   25-OCT-2017, entry version 39.
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   ECO:0000313|EMBL:EIF50505.1};
GN   ORFNames=SULAR_08482 {ECO:0000313|EMBL:EIF50505.1};
OS   Sulfurovum sp. AR.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Sulfurovum.
OX   NCBI_TaxID=1165841 {ECO:0000313|EMBL:EIF50505.1, ECO:0000313|Proteomes:UP000003180};
RN   [1] {ECO:0000313|EMBL:EIF50505.1, ECO:0000313|Proteomes:UP000003180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR {ECO:0000313|EMBL:EIF50505.1,
RC   ECO:0000313|Proteomes:UP000003180};
RX   PubMed=22815446; DOI=10.1128/JB.00741-12;
RA   Park S.J., Ghai R., Martin-Cuadrado A.B., Rodriguez-Valera F.,
RA   Jung M.Y., Kim J.G., Rhee S.K.;
RT   "Draft genome sequence of the sulfur-oxidizing bacterium "Candidatus
RT   Sulfurovum sediminum" AR, which belongs to the
RT   Epsilonproteobacteria.";
RL   J. Bacteriol. 194:4128-4129(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: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:EIF50505.1}.
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DR   EMBL; AJLE01000009; EIF50505.1; -; Genomic_DNA.
DR   RefSeq; WP_008245048.1; NZ_AJLE01000009.1.
DR   EnsemblBacteria; EIF50505; EIF50505; SULAR_08482.
DR   PATRIC; fig|1165841.3.peg.1696; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000003180; 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:UP000003180};
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:UP000003180}.
FT   DOMAIN      136    262       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      345    414       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     144    151       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   444 AA;  51202 MW;  4509C7D85A9B438F CRC64;
     MNIGQKVLFE LKKEITEVEY ERYIKNLTYD TKRSRSNIAY FNAPNMIIAK WIKSKYTDKL
     MHLFELQNEV KPEIEITVGK QKDQRSTPVT KHTSEKSHSK STYLNPSLTF ESFIVGDSNQ
     FAYTTAKSVA EKPGKLYNPL FLYGGVGLGK THLLQAIGNY HIDLGKTVIY TTLEQFMNSF
     TSHLRSQTMD RFREKFRECD LLLIDDIQFL SRKEQTQEEF FHTFNELYNN NKQIVITSDR
     QPNKIAGLVD RLRTRFEMGL LADIQPPGLE TKIAIIQKKC ELDGISLDNE IVNYIATHMG
     DNIREIEGTI IKLNALSSML NQEITLDFAQ NAIKDQLKEK KENITIDEIV KIISKELNIK
     PSDMKSKKRT KNVVNARRIA IYLARNLTPN SMPQIAVYFG MKDHTAISHA MKKINELIES
     DENFKVILEE LSNKVNTHTQ SDDI
//
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