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Database: UniProt
Entry: A0A0M4NX04_9GAMM
LinkDB: A0A0M4NX04_9GAMM
Original site: A0A0M4NX04_9GAMM 
ID   A0A0M4NX04_9GAMM        Unreviewed;       434 AA.
AC   A0A0M4NX04;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   16-JAN-2019, entry version 25.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=SP60_04015 {ECO:0000313|EMBL:ALE52452.1};
OS   Candidatus Thioglobus autotrophicus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Thioglobus.
OX   NCBI_TaxID=1705394 {ECO:0000313|EMBL:ALE52452.1};
RN   [1] {ECO:0000313|EMBL:ALE52452.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF1 {ECO:0000313|EMBL:ALE52452.1};
RX   PubMed=26494660;
RA   Shah V., Morris R.M.;
RT   "Genome Sequence of 'Candidatus Thioglobus autotrophica' Strain EF1, a
RT   Chemoautotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL   Genome Announc. 3:e01156-15(2015).
RN   [2] {ECO:0000313|EMBL:ALE52452.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EF1 {ECO:0000313|EMBL:ALE52452.1};
RX   PubMed=27434424;
RA   Shah V., Chang B.X., Morris R.M.;
RT   "Cultivation of a chemoautotroph from the SUP05 clade of marine
RT   bacteria that produces nitrite and consumes ammonium.";
RL   ISME J. 0:0-0(2016).
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:SAAS00756121}.
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}.
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DR   EMBL; CP010552; ALE52452.1; -; Genomic_DNA.
DR   RefSeq; WP_053951402.1; NZ_CP010552.1.
DR   EnsemblBacteria; ALE52452; ALE52452; SP60_04015.
DR   KEGG; tho:SP60_04015; -.
DR   PATRIC; fig|1705394.5.peg.804; -.
DR   KO; K02313; -.
DR   OrthoDB; 219876at2; -.
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; IPR018312; Chromosome_initiator_DnaA_CS.
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.
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:SAAS00756129};
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}.
FT   DOMAIN      126    259       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      342    411       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     134    141       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   434 AA;  48947 MW;  0E767E166FB46319 CRC64;
     MSKTWAQCLS TLKDTVSLSE YSVWIHPLKV LEDQHTLSLL APNTQVKNYI SKNLKTQIKN
     AVAQHNKNLK IFIGVAPSAN PEKANYKKHS TPLFEDYTFD NLVLGSANQM AYGATKQIAE
     NIKGSPYNPF IIYGGSGLGK THLMQAAGHL ARFQNPDMKV LYVPLMDFVR NITSSLRHNT
     IEDIKAFYQS ADLLLVDDIH LIAGKEKSQE EFFHIFNFLF NGKKQIIFTC DQPPKNIKSL
     EERLKTRFSQ GLNLHLTPPE LEMRAAILLK KSQDKKININ LTEDLALYIA GHITSNVRDL
     EGALLKLKAF VDFSKITQAF ISKEIVDAAL GDLIKPAIKN IEVNDVQKEV AKHYALTISD
     LSSKSRKQHV VLARQMAIYI CHELSALSLN KIGKQFGNRD HSTVIHAIKK IQEKLENSDI
     KNDYDLIKLK LANL
//
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