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Database: UniProt
Entry: A0A0X8HCK7_9GAMM
LinkDB: A0A0X8HCK7_9GAMM
Original site: A0A0X8HCK7_9GAMM 
ID   A0A0X8HCK7_9GAMM        Unreviewed;       488 AA.
AC   A0A0X8HCK7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   13-FEB-2019, entry version 24.
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   ECO:0000313|EMBL:AMD00163.1};
GN   ORFNames=LOKO_01086 {ECO:0000313|EMBL:AMD00163.1};
OS   Halomonas chromatireducens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=507626 {ECO:0000313|EMBL:AMD00163.1, ECO:0000313|Proteomes:UP000063387};
RN   [1] {ECO:0000313|EMBL:AMD00163.1, ECO:0000313|Proteomes:UP000063387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMD00163.1,
RC   ECO:0000313|Proteomes:UP000063387};
RX   PubMed=26988058;
RA   Sharko F.S., Shapovalova A.A., Tsygankova S.V., Komova A.V.,
RA   Boulygina E.S., Teslyuk A.B., Gotovtsev P.M., Namsaraev Z.B.,
RA   Khijniak T.V., Nedoluzhko A.V., Vasilov R.G.;
RT   "Draft Genome Sequence of 'Halomonas chromatireducens' Strain AGD 8-3,
RT   a Haloalkaliphilic Chromate- and Selenite-Reducing
RT   Gammaproteobacterium.";
RL   Genome Announc. 4:0-0(2016).
RN   [2] {ECO:0000313|EMBL:AMD00163.1, ECO:0000313|Proteomes:UP000063387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMD00163.1,
RC   ECO:0000313|Proteomes:UP000063387};
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, 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; CP014226; AMD00163.1; -; Genomic_DNA.
DR   RefSeq; WP_066446042.1; NZ_CP014226.1.
DR   EnsemblBacteria; AMD00163; AMD00163; LOKO_01086.
DR   KEGG; hco:LOKO_01086; -.
DR   PATRIC; fig|507626.3.peg.1077; -.
DR   KO; K02313; -.
DR   OrthoDB; 219876at2; -.
DR   BioCyc; GCF_001545155:G1EQ5-1086-MONOMER; -.
DR   Proteomes; UP000063387; Chromosome.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000063387};
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:UP000063387}.
FT   DOMAIN      185    401       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      396    465       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     193    200       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      347    367       {ECO:0000256|SAM:Coils}.
FT   COILED      465    485       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   488 AA;  54877 MW;  7D70F93AF1222D14 CRC64;
     MSLALWQKCL DFLQDELNAQ QFNTWIRPLQ AEEGESNELL LLAPNRFVRD WVGDKYAKRI
     NELLRDLAPA KPPRVVLTVG SRRAAAPRPR ELGAPVSASP RSPLGPAVHT PPRGDIGDER
     EIDRQREEGR SARRATGERE VQVEGSLKHN SGLNPNFTFE TFVEGKSNQL ARAASRQVSE
     NPGGAYNPLF LYGGVGLGKT HLMHAVGNAL ATRRENATVV YLHSERFVAD MVKALQLNAI
     NDFKRFYRSV DALLIDDIQF FAGKERSQEE FFHTFNALLE GGQQMILTSD RYPKEISGVE
     ERLKSRFGWG LTVAIEPPEL ETRVAILMKK ADQAKVDLPH DAAFFIAQKI RSNVRELEGA
     LKKVIADSHF MGKPITQDFI RESLKDLLAL QDKQVGVDNI QRTVAEYYKI KLSDLLSKRR
     SRSVARPRQV AMALAKELTN HSLPEIGDAF GGRDHTTVLH ACRKVLALQE ENADIREDYK
     NLLRLLTS
//
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