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Database: UniProt
Entry: A0A139SM16_9BACT
LinkDB: A0A139SM16_9BACT
Original site: A0A139SM16_9BACT 
ID   A0A139SM16_9BACT        Unreviewed;       490 AA.
AC   A0A139SM16;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   13-FEB-2019, entry version 21.
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   ORFNames=AXK12_04975 {ECO:0000313|EMBL:KXU35605.1};
OS   Cephaloticoccus capnophilus.
OC   Bacteria; Verrucomicrobia; Opitutae; Opitutales; Opitutaceae;
OC   Cephaloticoccus.
OX   NCBI_TaxID=1548208 {ECO:0000313|EMBL:KXU35605.1, ECO:0000313|Proteomes:UP000071392};
RN   [1] {ECO:0000313|EMBL:KXU35605.1, ECO:0000313|Proteomes:UP000071392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CV41 {ECO:0000313|EMBL:KXU35605.1,
RC   ECO:0000313|Proteomes:UP000071392};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) 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}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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:KXU35605.1}.
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DR   EMBL; LSZP01000037; KXU35605.1; -; Genomic_DNA.
DR   RefSeq; WP_068711863.1; NZ_LSZP01000037.1.
DR   EnsemblBacteria; KXU35605; KXU35605; AXK12_04975.
DR   BioCyc; GCF_001580045:AXK12_RS04440-MONOMER; -.
DR   Proteomes; UP000071392; 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   Gene3D; 3.30.300.180; -; 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; IPR013317; DnaA.
DR   InterPro; IPR013159; DnaA_C.
DR   InterPro; IPR024633; DnaA_N_dom.
DR   InterPro; IPR038454; DnaA_N_sf.
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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756129};
KW   Complete proteome {ECO:0000313|Proteomes:UP000071392};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000071392}.
FT   DOMAIN      186    315       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      398    467       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     194    201       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   490 AA;  54353 MW;  784B21149158B2FC CRC64;
     MPTATLAPSP WETAKTSLKQ FFSEDVFKMW FEPLHCIELG EDTITLGVPN DFAAIWIQEN
     YLDLISKHLS LAYGRELSIT LQKAAPPQSA HAHRGHSDSA ALLDGQGNAR GSSGAVSGGR
     GVNDHAQTGT GFDRDASPRL GAAAPERRRP EATLNPRNTF DTLVVGANNQ MAHAAAMAVA
     QAPAQAYNPL FLYGDTGLGK THLMHAIGHA ILQNRPDARV VYLSTERFTN EFIQALQENS
     LTKFRQRYRR ASVLLLDDVQ FLAGKERIQE EFFHTFNDLF ESGKQIVLSS DRRASEIQQL
     EARLVSRFEW GLPADIQAPD YETRVAILRS KAATLKADVP HEVITFIAQR LSGNVRRLEG
     ALIKVSSYAA LTGRPLDIPT AEKLLQDVLI EQAQNLLTID VIQKRVADHF QIRHSDMTSK
     RRPNNIAIPR QIAMFLSRKL TKHSLQDIGD AFGGRDHGTV IHACKAVDNM IEQDPSMRGS
     IEFLKTQLAR
//
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